DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
Heterodimeric transcription factors containing a DNA-binding alpha subunits, (CORE BINDING FACTOR ALPHA SUBUNITS), along with a non-DNA-binding beta subunits, CORE BINDING FACTOR BETA SUBUNIT. Core Binding Factor regulates GENETIC TRANSCRIPTION of a variety of GENES involved primarily in CELL DIFFERENTIATION and CELL CYCLE progression.
A general transcription factor that plays a major role in the activation of eukaryotic genes transcribed by RNA POLYMERASES. It binds specifically to the TATA BOX promoter element, which lies close to the position of transcription initiation in RNA transcribed by RNA POLYMERASE II. Although considered a principal component of TRANSCRIPTION FACTOR TFIID it also takes part in general transcription factor complexes involved in RNA POLYMERASE I and RNA POLYMERASE III transcription.
A conserved A-T rich sequence which is contained in promoters for RNA polymerase II. The segment is seven base pairs long and the nucleotides most commonly found are TATAAAA.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
The major sequence-specific DNA-binding component involved in the activation of transcription of RNA POLYMERASE II. It was originally described as a complex of TATA-BOX BINDING PROTEIN and TATA-BINDING PROTEIN ASSOCIATED FACTORS. It is now know that TATA BOX BINDING PROTEIN-LIKE PROTEINS may take the place of TATA-box binding protein in the complex.
A non-DNA binding transcription factor that is a subunit of core binding factor. It forms heterodimeric complexes with CORE BINDING FACTOR ALPHA SUBUNITS, and regulates GENETIC TRANSCRIPTION of a variety of GENES involved primarily in CELL DIFFERENTIATION and CELL CYCLE progression.
A heterotrimeric DNA-binding protein that binds to CCAAT motifs in the promoters of eukaryotic genes. It is composed of three subunits: A, B and C.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Factors that form a preinitiation complex at promoters that are specifically transcribed by RNA POLYMERASE I.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A family of transcription factors that bind to the cofactor CORE BINDING FACTOR BETA SUBUNIT to form core binding factor. Family members contain a highly conserved DNA-binding domain known as the runt domain. They can act as both activators and repressors of expression of GENES involved in CELL DIFFERENTIATION and CELL CYCLE progression.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
An RNA POLYMERASE II specific transcription factor. It may play a role in transcriptional activation of gene expression by interacting with the TATA-BOX BINDING PROTEIN component of TRANSCRIPTION FACTOR TFIID.
A ubiquitously expressed telomere-binding protein that is present at TELOMERES throughout the CELL CYCLE. It is a suppressor of telomere elongation and may be involved in stabilization of telomere length. It is structurally different from TELOMERIC REPEAT BINDING PROTEIN 2 in that it contains acidic N-terminal amino acid residues.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
Factors that associate with TATA-BOX BINDING PROTEIN. Many of them are components of TRANSCRIPTION FACTOR TFIID
A class of proteins that were originally identified by their ability to bind the DNA sequence CCAAT. The typical CCAAT-enhancer binding protein forms dimers and consists of an activation domain, a DNA-binding basic region, and a leucine-rich dimerization domain (LEUCINE ZIPPERS). CCAAT-BINDING FACTOR is structurally distinct type of CCAAT-enhancer binding protein consisting of a trimer of three different subunits.
A class of proteins related in structure and function to TATA-BOX BINDING PROTEIN that can take the place of TATA-BOX BINDING PROTEIN in the transcription initiation complex. They are found in most multicellular organisms and may be involved in tissue-specific promoter regulation. They bind to DNA and interact with TATA-BINDING PROTEIN ASSOCIATED FACTORS, however they may lack specificity for the TATA-BOX.
A family of transcription factors found primarily in PLANTS that bind to the G-box DNA sequence CACGTG or to a consensus sequence CANNTG.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
An RNA POLYMERASE II specific transcription factor. It plays a role in assembly of the pol II transcriptional preinitiation complex and has been implicated as a target of gene-specific transcriptional activators.
A transcription factor that dimerizes with the cofactor CORE BINDING FACTOR BETA SUBUNIT to form core binding factor. It contains a highly conserved DNA-binding domain known as the runt domain. Runx1 is frequently mutated in human LEUKEMIAS.
Promoter-specific RNA polymerase II transcription factor that binds to the GC box, one of the upstream promoter elements, in mammalian cells. The binding of Sp1 is necessary for the initiation of transcription in the promoters of a variety of cellular and viral GENES.
Established cell cultures that have the potential to propagate indefinitely.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A ubiquitously expressed telomere-binding protein that is present at TELOMERES throughout the cell cycle. It is a suppressor of telomere elongation and may be involved in stabilization of telomere length. It is structurally different from TELOMERIC REPEAT BINDING PROTEIN 1 in that it contains basic N-terminal amino acid residues.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The so-called general transcription factors that bind to RNA POLYMERASE II and that are required to initiate transcription. They include TFIIA; TFIIB; TFIID; TFIIE; TFIIF; TFIIH; TFII-I; and TFIIJ. In vivo they apparently bind in an ordered multi-step process and/or may form a large preinitiation complex called RNA polymerase II holoenzyme.
A transcription factor that dimerizes with CORE BINDING FACTOR BETA SUBUNIT to form core binding factor. It contains a highly conserved DNA-binding domain known as the runt domain and is involved in genetic regulation of skeletal development and CELL DIFFERENTIATION.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. The enzyme functions in the nucleolar structure and transcribes DNA into RNA. It has different requirements for cations and salts than RNA polymerase II and III and is not inhibited by alpha-amanitin. EC 2.7.7.6.
Cis-acting DNA sequences which can increase transcription of genes. Enhancers can usually function in either orientation and at various distances from a promoter.
A family of DNA binding proteins that regulate expression of a variety of GENES during CELL DIFFERENTIATION and APOPTOSIS. Family members contain a highly conserved carboxy-terminal basic HELIX-TURN-HELIX MOTIF involved in dimerization and sequence-specific DNA binding.
Nucleic acid sequences involved in regulating the expression of genes.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Within most types of eukaryotic CELL NUCLEUS, a distinct region, not delimited by a membrane, in which some species of rRNA (RNA, RIBOSOMAL) are synthesized and assembled into ribonucleoprotein subunits of ribosomes. In the nucleolus rRNA is transcribed from a nucleolar organizer, i.e., a group of tandemly repeated chromosomal genes which encode rRNA and which are transcribed by RNA polymerase I. (Singleton & Sainsbury, Dictionary of Microbiology & Molecular Biology, 2d ed)
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Proteins secreted by the prostate gland. The major secretory proteins from the human prostate gland include PROSTATE-SPECIFIC ANTIGEN, prostate-specific acid phosphatase, prostate-specific membrane antigen, and prostate-specific protein-94.
A family of double-stranded RNA-binding proteins that are related to NFATC TRANSCRIPTION FACTORS. In addition to binding to RNA, nuclear factor 90 proteins form heterodimeric complexes that regulate GENETIC TRANSCRIPTION and may play a role in T-CELL activation.
The chromosome region which is active in nucleolus formation and which functions in the synthesis of ribosomal RNA.
The most abundant form of RNA. Together with proteins, it forms the ribosomes, playing a structural role and also a role in ribosomal binding of mRNA and tRNAs. Individual chains are conventionally designated by their sedimentation coefficients. In eukaryotes, four large chains exist, synthesized in the nucleolus and constituting about 50% of the ribosome. (Dorland, 28th ed)
A T-cell factor that plays an essential role in EMBRYONIC DEVELOPMENT.
An enzyme capable of hydrolyzing highly polymerized DNA by splitting phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide. This catalyzes endonucleolytic cleavage of DNA yielding 5'-phosphodi- and oligonucleotide end-products. The enzyme has a preference for double-stranded DNA.
Synthetic or natural oligonucleotides used in hybridization studies in order to identify and study specific nucleic acid fragments, e.g., DNA segments near or within a specific gene locus or gene. The probe hybridizes with a specific mRNA, if present. Conventional techniques used for testing for the hybridization product include dot blot assays, Southern blot assays, and DNA:RNA hybrid-specific antibody tests. Conventional labels for the probe include the radioisotope labels 32P and 125I and the chemical label biotin.
An electrophoretic technique for assaying the binding of one compound to another. Typically one compound is labeled to follow its mobility during electrophoresis. If the labeled compound is bound by the other compound, then the mobility of the labeled compound through the electrophoretic medium will be retarded.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
Myosin type II isoforms found in smooth muscle.
A terminal section of a chromosome which has a specialized structure and which is involved in chromosomal replication and stability. Its length is believed to be a few hundred base pairs.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
DNA sequences encoding RIBOSOMAL RNA and the segments of DNA separating the individual ribosomal RNA genes, referred to as RIBOSOMAL SPACER DNA.
A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.
A heterogeneous-nuclear ribonucleoprotein that has specificity for AU-rich elements found in the 3'-region of mRNA and may play a role in RNA stability. Several isoforms of hnRNP D protein have been found to occur due to alternative mRNA splicing (RNA SPLICING).
A method for determining the sequence specificity of DNA-binding proteins. DNA footprinting utilizes a DNA damaging agent (either a chemical reagent or a nuclease) which cleaves DNA at every base pair. DNA cleavage is inhibited where the ligand binds to DNA. (from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.
Proteins that specifically bind to TELOMERES. Proteins in this class include those that perform functions such as telomere capping, telomere maintenance and telomere stabilization.
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
A ubiquitously expressed sequence-specific transcriptional repressor that is normally the target of signaling by NOTCH PROTEINS.
A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.
A family of low-molecular weight, non-histone proteins found in chromatin.
A plant genus of the family ERICACEAE known for species with edible fruits.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
Nucleotide sequences, usually upstream, which are recognized by specific regulatory transcription factors, thereby causing gene response to various regulatory agents. These elements may be found in both promoter and enhancer regions.
A plant species of the genus VACCINIUM.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
A family of transcription factors that contain regions rich in basic residues, LEUCINE ZIPPER domains, and HELIX-LOOP-HELIX MOTIFS.
Adaptation to a new environment or to a change in the old.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A specific pair of GROUP E CHROMOSOMES of the human chromosome classification.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Liquids transforming into solids by the removal of heat.
A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.
Genes which regulate or circumscribe the activity of other genes; specifically, genes which code for PROTEINS or RNAs which have GENE EXPRESSION REGULATION functions.
An aberration in which a chromosomal segment is deleted and reinserted in the same place but turned 180 degrees from its original orientation, so that the gene sequence for the segment is reversed with respect to that of the rest of the chromosome.
Deletion of sequences of nucleic acids from the genetic material of an individual.
An absence of warmth or heat or a temperature notably below an accustomed norm.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Ubiquitously expressed basic HELIX-LOOP-HELIX MOTIF transcription factors. They bind CANNTG sequences in the promoters of a variety of GENES involved in carbohydrate and lipid metabolism.
Proteins encoded by homeobox genes (GENES, HOMEOBOX) that exhibit structural similarity to certain prokaryotic and eukaryotic DNA-binding proteins. Homeodomain proteins are involved in the control of gene expression during morphogenesis and development (GENE EXPRESSION REGULATION, DEVELOPMENTAL).
DNA locations with the consensus sequence CANNTG. ENHANCER ELEMENTS may contain multiple copies of this element. E-boxes play a regulatory role in the control of transcription. They bind with basic helix-loop-helix (bHLH) type TRANSCRIPTION FACTORS. Binding specificity is determined by the specific bHLH heterodimer or homodimer combination and by the specific nucleotides at the 3rd and 4th position of the E-box sequence.
Proteins found in any species of fungus.

Transcriptional repression of human hepatitis B virus genes by a bZIP family member, E4BP4. (1/138)

Box alpha is an essential element of both the upstream regulatory sequence of the core promoter and the second enhancer, which positively regulate the transcription of human hepatitis B virus (HBV) genes. In this paper, we describe the cloning and characterization of a box alpha binding protein, E4BP4. E4BP4 is a bZIP type of transcription factor. Overexpression of E4BP4 represses the stimulating activity of box alpha in the upstream regulatory sequence of the core promoter and the second enhancer in differentiated human hepatoma cell lines. E4BP4 can also suppress the transcription of HBV genes and the production of HBV virions in a transient-transfection system that mimics the viral infection in vivo. Expression of an E4BP4 antisense transcript can, instead, elevate the transcription of the core promoter. A low abundance of E4BP4 protein and mRNA in differentiated human hepatoma cell lines is detected, and E4BP4 is not a major component of box alpha binding proteins in untransfected differentiated human hepatoma cell lines. C/EBPalpha and C/EBPbeta, in contrast, are major components of the box alpha binding activity present in nuclear extracts. E4BP4 has a stronger binding affinity towards box alpha than the endogenous box alpha binding activity present in nuclear extracts. Structure and function analysis of E4BP4 reveals that DNA binding activity is sufficient to confer the negative regulatory function of E4BP4. These results indicate that binding site occlusion is the mechanism whereby E4BP4 suppresses transcription in HBV.  (+info)

Two distinct interleukin-3-mediated signal pathways, Ras-NFIL3 (E4BP4) and Bcl-xL, regulate the survival of murine pro-B lymphocytes. (2/138)

Hematopoietic cells require cytokine-initiated signals for survival as well as proliferation. The pathways that transduce these signals, ensuring timely regulation of cell fate genes, remain largely undefined. The NFIL3 (E4BP4) transcription factor, Bcl-xL, and constitutively active mutants of components in Ras signal transduction pathways have been identified as key regulation proteins affecting murine interleukin-3 (IL-3)-dependent cell survival. Here we show that expression of NFIL3 is regulated by oncogenic Ras mutants through both the Raf-mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways. NFIL3 inhibits apoptosis without affecting Bcl-xL expression. By contrast, Bcl-xL levels are regulated through the membrane proximal portion in the cytoplasmic domain of the receptor (betac chain), which is shared by IL-3 and granulocyte-macrophage colony-stimulating factor. Activation of either pathway alone is insufficient to ensure cell survival, indicating that multiple independent signal transduction pathways mediate the survival of developing B-lymphoid cells.  (+info)

Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2. (3/138)

Herpes simplex virus infection is initiated by VP16, a viral transcription factor that activates the viral immediate-early (IE) genes. VP16 does not recognize the IE gene promoters directly but instead forms a multiprotein complex with Oct-1 and HCF-1, a ubiquitous nuclear protein required for progression through the G1 phase of the cell cycle. The functional significance of recruiting HCF-1 to the VP16-induced complex is not understood. Here we describe the identification of a second HCF-like protein, designated HCF-2. HCF-2 is smaller than HCF-1 but shares three regions of strong amino acid sequence homology, including the beta-propeller domain required for association with VP16. HCF-2 is expressed in many tissues, especially the testis, and shows a more dynamic pattern of subcellular localization than HCF-1. Although HCF-2 associates with VP16 and can support complex assembly with Oct-1 and DNA, it is significantly less efficient than HCF-1. A similar preference is shown by LZIP, a cellular counterpart of VP16. Analysis of chimeric proteins showed that differences between the fifth and sixth kelch repeats of the beta-propeller domains from HCF-1 and HCF-2 dictate this selectivity. These results reveal an unexpected level of specificity in the recruitment of HCF-1 to the VP16-induced complex, paralleling the preferential selection of Oct-1 rather than the closely related POU domain protein Oct-2. Implications for regulation of the viral life cycle are discussed.  (+info)

Ubiquitination and degradation of ATF2 are dimerization dependent. (4/138)

Ubiquitination and proteasome-dependent degradation are key determinants of the half-lives of many transcription factors. Homo- or heterodimerization of basic region-leucine zipper (bZIP) transcription factors is required for their transcriptional activities. Here we show that activating transcription factor 2 (ATF2) heterodimerization with specific bZIP proteins is an important determinant of the ubiquitination and proteasome-dependent degradation of ATF2. Depletion of c-Jun as one of the ATF2 heterodimer partners from the targeting proteins decreased the efficiency of ATF2 ubiquitination in vitro, whereas the addition of exogenously purified c-Jun restored it. Similarly, overexpression of c-Jun in 293T human embryo kidney cells increased ATF2 ubiquitination in vivo and reduced its half-life in a dose-dependent manner. Mutations of ATF2 that disrupt its dimerization inhibited ATF2 ubiquitination in vitro and in vivo. Conversely, removal of residues 150 to 248, as in a constitutively active ATF2 spliced form, enhanced ATF2 dimerization and transactivation, which coincided with increased ubiquitination and decreased stability. Our findings indicate the increased sensitivity of transcriptionally active dimers of ATF2 to ubiquitination and proteasome-dependent degradation. Based on these observations, we conclude that increased targeting of a transcriptionally active ATF2 form indicates the mechanism by which the magnitude and the duration of the cellular stress response are regulated.  (+info)

GC factor 2 represses platelet-derived growth factor A-chain gene transcription and is itself induced by arterial injury. (5/138)

Platelet-derived growth factor (PDGF) is a mitogen and chemoattractant for a wide variety of cell types. The genes encoding PDGF A chain (PDGF-A) and PDGF B chain (PDGF-B) reside on separate chromosomes and are independently regulated at the level of transcription. Regulatory events underlying inducible PDGF-A expression have been the focus of much investigation. However, mechanisms that inhibit transcription of this gene are not well understood. In this study, we report the capacity of a newly cloned DNA binding factor, GC factor 2 (GCF2), to repress expression driven by the human PDGF-A promoter. 5' Deletion and transient cotransfection analysis in vascular endothelial cells revealed that GCF2 repression is mediated by a nucleotide region located in the proximal region of the PDGF-A promoter. Electrophoretic mobility shift assays demonstrate that GCF2 binds to this region in a specific and dose-dependent manner. Interestingly, the site bound by GCF2 overlaps those for specificity protein-1 (Sp1) and early growth response factor-1 (Egr-1), zinc finger transcription factors that direct basal and inducible expression of the PDGF-A gene. Gel shift experiments revealed that GCF2 competes with these factors for interaction with the PDGF-A promoter. Overexpression of GCF2 suppressed endogenous PDGF-A expression in vascular endothelial cells and smooth muscle cells. GCF2 was induced on mechanical injury of cells in culture as well as after balloon injury of the rat carotid artery wall. Time course studies revealed the sustained induction of GCF2 after injury while PDGF-A levels sharply returned to baseline. Smooth muscle cell proliferation was inhibited by GCF2, an effect reversed by the addition of exogenous PDGF-AA. These findings demonstrate negative regulation of PDGF-A expression by GCF2. This is the first report of the induction of an endogenous transcriptional repressor in the rat vessel wall.  (+info)

Identification of cis-regulating elements and trans-acting factors regulating the expression of the gene encoding the small subunit of ribonucleotide reductase in Dictyostelium discoideum. (6/138)

We have examined the promoter of rnrB, the gene encoding the small subunit of ribonucleotide reductase of Dictyostelium discoideum, using lacZ as a reporter gene. Deletion analysis showed that expression of this gene in vegetative cells involves an A/T-rich element, whereas its expression in prespore cells during development requires a region encompassing two G/C-rich elements, designated box A and box B. Removal of boxes A and B results in very low level of activity. When either box A or box B is deleted, prestalk cells adjacent to the prespore zone also express beta-galactosidase. The behavior of these cis-regulatory elements implies that the mechanism regulating the prespore-specific expression of rnrB is different from that regulating other known prespore genes. We have used electrophoretic mobility shift assays to identify factors that interact with box A and box B. Box A interacts with a factor that is found in the nuclear fraction. While box B interacts with a factor that is present in the cytosolic fraction throughout growth and development, its presence in the nuclear fraction is developmentally regulated. Results from competition assays suggest that both box A and box B interact with transcriptional activators that have not been characterized previously.  (+info)

Reduction of G-box binding factor DNA binding activity, but not G-box binding factor abundance, causes the downregulation of RBCS2 expression during early tomato fruit development. (7/138)

The downregulation of RBCS2 promoter activity during tomato fruit development has been investigated by transient gene expression. A major drop in promoter activity occurs between 5 and 25 mm fruit diameter, corresponding to the late cell division to early cell enlargement phase. This drop is abolished by a mutation of the single G-box element necessary for high RBCS2 promoter activity in young tomato fruit. The G-box binding activity of fruit nuclear and total protein extracts drops concomitantly with the reduction of RBCS2 promoter activity while G-box binding factor expression is not affected. The data indicate that the developmental signal that downregulates the RBCS2 promoter acts on the regulation of DNA binding activity of constitutively expressed G-box binding factors.  (+info)

CHOP enhancement of gene transcription by interactions with Jun/Fos AP-1 complex proteins. (8/138)

The transcription factor CHOP (C/EBP homologous protein 10) is a bZIP protein induced by a variety of stimuli that evoke cellular stress responses and has been shown to arrest cell growth and to promote programmed cell death. CHOP cannot form homodimers but forms stable heterodimers with the C/EBP family of activating transcription factors. Although initially characterized as a dominant negative inhibitor of C/EBPs in the activation of gene transcription, CHOP-C/EBP can activate certain target genes. Here we show that CHOP interacts with members of the immediate-early response, growth-promoting AP-1 transcription factor family, JunD, c-Jun, and c-Fos, to activate promoter elements in the somatostatin, JunD, and collagenase genes. The leucine zipper dimerization domain is required for interactions with AP-1 proteins and transactivation of transcription. Analyses by electrophoretic mobility shift assays and by an in vivo mammalian two-hybrid system for protein-protein interactions indicate that CHOP interacts with AP-1 proteins inside cells and suggest that it is recruited to the AP-1 complex by a tethering mechanism rather than by direct binding of DNA. Thus, CHOP not only is a negative or a positive regulator of C/EBP target genes but also, when tethered to AP-1 factors, can activate AP-1 target genes. These findings establish the existence of a new mechanism by which CHOP regulates gene expression when cells are exposed to cellular stress.  (+info)

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

Core binding factors (CBFs) are a group of proteins that play critical roles in the development and differentiation of hematopoietic cells, which are the cells responsible for the formation of blood and immune systems. The term "core binding factor" refers to the ability of these proteins to bind to specific DNA sequences, known as core binding sites, and regulate gene transcription.

The two main CBFs are:

1. Core Binding Factor Alpha (CBF-α): Also known as RUNX1 or AML1, this protein forms a complex with Core Binding Factor Beta (CBF-β) to regulate the expression of genes involved in hematopoiesis. Mutations in CBF-α have been associated with various types of leukemia and myelodysplastic syndromes.
2. Core Binding Factor Beta (CBF-β): Also known as PEBP2B, this protein partners with CBF-α to form the active transcription factor complex. CBF-β enhances the DNA binding affinity and stability of the CBF-α/CBF-β heterodimer.

In certain types of leukemia, chromosomal abnormalities can lead to the formation of fusion proteins involving CBF-α or CBF-β. These fusion proteins disrupt normal hematopoiesis and contribute to the development of cancer. Examples include the t(8;21) translocation that creates the AML1/ETO fusion protein in acute myeloid leukemia (AML) and the inv(16) inversion that forms the CBFB-MYH11 fusion protein in AML.

The TATA-box binding protein (TBP) is a general transcription factor that plays a crucial role in the initiation of transcription of protein-coding genes in archaea and eukaryotes. It is named after its ability to bind to the TATA box, a conserved DNA sequence found in the promoter regions of many genes.

TBP is a key component of the transcription preinitiation complex (PIC), which also includes other general transcription factors and RNA polymerase II in eukaryotes. The TBP protein has a unique structure, characterized by a saddle-shaped DNA-binding domain that allows it to recognize and bind to the TATA box in a sequence-specific manner.

By binding to the TATA box, TBP helps to position the RNA polymerase II complex at the start site of transcription, allowing for the initiation of RNA synthesis. TBP also plays a role in regulating gene expression by interacting with various coactivators and corepressors that modulate its activity.

Mutations in the TBP gene have been associated with several human diseases, including some forms of cancer and neurodevelopmental disorders.

I'm sorry for any confusion, but "TATA box" is actually a term used in molecular biology, specifically in the field of genetics and gene regulation. It does not have a direct medical definition.

The TATA box is a DNA sequence located in the promoter region of many genes, which serves as a binding site for certain proteins involved in the initiation of transcription. Transcription is the first step in gene expression, where the information in a gene is used to create a corresponding protein or RNA molecule.

The TATA box is typically found about 25-30 base pairs upstream of the transcription start site and has the consensus sequence "TATAAA". It is recognized by the TATA-binding protein (TBP), which is a component of the transcription factor II D (TFIIB) complex. The binding of TBP to the TATA box helps to position the RNA polymerase enzyme properly for the initiation of transcription.

While not a medical term per se, understanding the function of the TATA box and other cis-acting elements in gene regulation is important for understanding how genes are turned on and off in various cellular processes and how this can go awry in certain diseases.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

Transcription Factor TFIID is a multi-subunit protein complex that plays a crucial role in the process of transcription, which is the first step in gene expression. In eukaryotic cells, TFIID is responsible for recognizing and binding to the promoter region of genes, specifically to the TATA box, a sequence found in many promoters that acts as a binding site for the general transcription factors.

TFIID is composed of the TATA-box binding protein (TBP) and several TBP-associated factors (TAFs). The TBP subunit initially recognizes and binds to the TATA box, followed by the recruitment of other general transcription factors and RNA polymerase II to form a preinitiation complex. This complex then initiates the transcription of DNA into messenger RNA (mRNA), allowing for the production of proteins and the regulation of gene expression.

Transcription Factor TFIID is essential for accurate and efficient transcription, and its dysfunction can lead to various developmental and physiological abnormalities, including diseases such as cancer.

Core Binding Factor-beta (CBF-β) is a subunit of the Core Binding Factor (CBF), which is a heterodimeric transcription factor composed of a DNA-binding alpha subunit and a non-DNA binding beta subunit. The CBF plays a crucial role in hematopoiesis, the process of blood cell development, by regulating the expression of various genes involved in this process.

The CBF-β subunit is a 36 kDa protein that is encoded by the CBFB gene in humans. It does not bind to DNA directly but instead forms a complex with the DNA-binding alpha subunit, which is either RUNX1 (also known as AML1), RUNX2, or RUNX3. The CBF-β subunit stabilizes the interaction between the alpha subunit and DNA, enhances its DNA-binding affinity, and increases the transcriptional activity of the complex.

Mutations in the CBFB gene have been associated with several hematological disorders, including acute myeloid leukemia (AML), myelodysplastic syndromes (MDS), and familial platelet disorder with predisposition to AML (FPD/AML). These mutations can lead to aberrant transcriptional regulation of hematopoietic genes, resulting in the development of these disorders.

CCAAT-binding factor (CBF) is a transcription factor that binds to the CCAAT box, a specific DNA sequence found in the promoter regions of many genes. The CBF complex is composed of three subunits, NF-YA, NF-YB, and NF-YC, which are required for its DNA binding activity. The CBF complex plays important roles in various biological processes, including cell cycle regulation, differentiation, and stress response.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

POL1 (Polymerase 1) Transcription Initiation Complex Proteins are a set of proteins that come together to form the initiation complex for the transcription of ribosomal RNA (rRNA) genes in eukaryotic cells. The POL1 complex includes RNA polymerase I, select transcription factors, and other regulatory proteins. This complex is responsible for the transcription of rRNA genes located within the nucleolus, a specialized region within the cell nucleus. Proper assembly and functioning of this initiation complex are crucial for the production of ribosomes, which play a critical role in protein synthesis.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Core Binding Factor (CBF) is a transcription factor that plays a crucial role in the development and differentiation of various tissues, including hematopoietic cells. It is composed of two subunits: alpha (CBFA or AML1) and beta (CBFB or PEBP2b).

The CBFA subunit, also known as RUNX1, is a transcription factor that binds to DNA and regulates the expression of target genes involved in hematopoiesis, neurogenesis, and other developmental processes. It contains a highly conserved DNA-binding domain called the runt homology domain (RHD) that recognizes specific DNA sequences.

Mutations in CBFA have been associated with various hematological disorders, including acute myeloid leukemia (AML), myelodysplastic syndrome (MDS), and familial platelet disorder with predisposition to AML (FDPA). These mutations can lead to altered gene expression, impaired differentiation, and increased proliferation of hematopoietic cells, contributing to the development of these diseases.

Transcriptional activation is the process by which a cell increases the rate of transcription of specific genes from DNA to RNA. This process is tightly regulated and plays a crucial role in various biological processes, including development, differentiation, and response to environmental stimuli.

Transcriptional activation occurs when transcription factors (proteins that bind to specific DNA sequences) interact with the promoter region of a gene and recruit co-activator proteins. These co-activators help to remodel the chromatin structure around the gene, making it more accessible for the transcription machinery to bind and initiate transcription.

Transcriptional activation can be regulated at multiple levels, including the availability and activity of transcription factors, the modification of histone proteins, and the recruitment of co-activators or co-repressors. Dysregulation of transcriptional activation has been implicated in various diseases, including cancer and genetic disorders.

Transcription Factor TFIIA is not a specific transcription factor itself, but rather a general term that refers to one of the several protein complexes that make up the larger Preinitiation Complex (PIC) in eukaryotic transcription. The PIC is responsible for the accurate initiation of transcription by RNA polymerase II, which transcribes most protein-coding genes in eukaryotes.

TFIIA is a heterotrimeric complex composed of three subunits: TAF1 (also known as TCP14/TCP22), TAF2 (also known as TCP80), and TAF3 (also known as GTF2A1). It plays a crucial role in the early stages of transcription initiation by helping to stabilize the binding of RNA polymerase II to the promoter region of the gene, as well as facilitating the correct positioning of other general transcription factors.

In addition to its role in the PIC, TFIIA has also been shown to have a function in regulating chromatin structure and accessibility, which can impact gene expression. Overall, Transcription Factor TFIIA is an essential component of the eukaryotic transcription machinery that helps ensure accurate and efficient initiation of gene transcription.

Telomeric Repeat Binding Protein 1 (TRF1) is a protein that binds to the telomeres, which are the repetitive DNA sequences found at the ends of chromosomes. TRF1 plays a crucial role in the protection and regulation of telomere length. It helps to form a protective cap on the end of the chromosome, preventing it from being recognized as damaged or broken. Additionally, TRF1 is involved in the negative regulation of telomerase, an enzyme that adds repetitive DNA sequences to the ends of chromosomes, thereby controlling the length of the telomeres. Mutations in TRF1 have been associated with certain types of cancer and premature aging disorders.

Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

TATA-binding protein associated factors (TAFs) are a group of proteins that associate with the TATA-binding protein (TBP) to form the basal transcription complex, which is involved in the initiation of gene transcription. In eukaryotes, TBP is a general transcription factor that recognizes and binds to the TATA box, a conserved DNA sequence found in the promoter regions of many genes. TAFs interact with TBP and other proteins to form the multi-subunit complex known as TFIID (transcription factor II D).

TAFs can be classified into two categories: TAF1 subunits and TAF2 subunits. The TAF1 subunits are characterized by a conserved histone fold motif, which is also found in the core histones of nucleosomes. These TAF1 subunits play a role in stabilizing the interaction between TBP and DNA, as well as recruiting additional transcription factors to the promoter. The TAF2 subunits, on the other hand, do not contain the histone fold motif and are involved in mediating interactions with other proteins and regulatory elements.

Together, TBP and TAFs help to position the RNA polymerase II enzyme at the start site of transcription and facilitate the assembly of the pre-initiation complex (PIC), which includes additional general transcription factors and mediator proteins. The PIC then initiates the synthesis of mRNA, allowing for the expression of specific genes.

In summary, TATA-binding protein associated factors are a group of proteins that associate with TBP to form the basal transcription complex, which plays a crucial role in the initiation of gene transcription by recruiting RNA polymerase II and other general transcription factors to the promoter region.

CCAAT-Enhancer-Binding Proteins (C/EBPs) are a family of transcription factors that play crucial roles in the regulation of various biological processes, including cell growth, development, and differentiation. They bind to specific DNA sequences called CCAAT boxes, which are found in the promoter or enhancer regions of many genes.

The C/EBP family consists of several members, including C/EBPα, C/EBPβ, C/EBPγ, C/EBPδ, and C/EBPε. These proteins share a highly conserved basic region-leucine zipper (bZIP) domain, which is responsible for their DNA-binding and dimerization activities.

C/EBPs can form homodimers or heterodimers with other bZIP proteins, allowing them to regulate gene expression in a combinatorial manner. They are involved in the regulation of various physiological processes, such as inflammation, immune response, metabolism, and cell cycle control. Dysregulation of C/EBP function has been implicated in several diseases, including cancer, diabetes, and inflammatory disorders.

TATA box binding protein-like proteins (TBP-like proteins or TBPLs) are a family of transcription factors that share structural and functional similarities with the TATA box binding protein (TBP). TBP is a critical component of the initiation complex that binds to the TATA box, a specific DNA sequence found in the promoter regions of many genes.

TBPLs are involved in regulating gene expression by recognizing and binding to specific DNA sequences, similar to TBP. However, TBPLs have distinct roles in transcriptional regulation compared to TBP. They can either act as activators or repressors of transcription, depending on the context and the target genes they interact with.

TBPLs are found in various organisms, including animals, plants, and fungi. In humans, there are three known TBPLs: TBPL1 (also known as TRF3), TBPL2 (also known as TRF2), and TBPL3 (also known as DR1). These proteins have been implicated in various cellular processes, such as development, differentiation, and stress response.

In summary, TATA box binding protein-like proteins are a family of transcription factors that share structural and functional similarities with TBP but have distinct roles in regulating gene expression.

I'm sorry for any confusion, but "G-Box Binding Factors" is not a widely recognized or established term in medical or molecular biology literature. The "G-box" is a specific sequence of DNA that can be found in the promoter regions of many genes and serves as a binding site for various transcription factors. Transcription factors are proteins that regulate gene expression by binding to specific DNA sequences and either promoting or inhibiting the initiation of transcription.

However, "G-Box Binding Factors" is too broad since multiple transcription factors can bind to the G-box sequence. Some examples of transcription factors known to bind to the G-box include proteins like GBF (G-box binding factor), HSF (heat shock transcription factor), and bZIP (basic region/leucine zipper) proteins, among others.

If you have a more specific context or reference related to "G-Box Binding Factors," I would be happy to help provide further information based on that context.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Transcription Factor IIB (TFIIB) is a general transcription factor that plays an essential role in the initiation of gene transcription by RNA polymerase II in eukaryotic cells. It is a small protein consisting of approximately 350 amino acids and has several functional domains, including a zinc-binding domain, a helix-turn-helix motif, and a cyclin-like fold.

TFIIB acts as a bridge between the RNA polymerase II complex and the promoter DNA, recognizing and binding to specific sequences in the promoter region known as the B recognition element (BRE) and the TATA box. By interacting with other transcription factors, such as TFIIF and TFIIH, TFIIB helps to position RNA polymerase II correctly on the promoter DNA and to unwind the double helix, allowing for the initiation of transcription.

TFIIB is a highly conserved protein across eukaryotes, and mutations in the gene encoding TFIIB have been associated with several human diseases, including developmental disorders and cancer.

Core Binding Factor Alpha 2 Subunit, also known as CBF-A2 or CEBP-α, is a protein that forms a complex with other proteins to act as a transcription factor. Transcription factors are proteins that help regulate the expression of genes by binding to specific DNA sequences and controlling the rate of transcription of genetic information from DNA to RNA.

CBF-A2 is a member of the CCAAT/enhancer-binding protein (C/EBP) family of transcription factors, which are important in regulating various biological processes such as cell growth, development, and inflammation. CBF-A2 forms a heterodimer with Core Binding Factor Beta (CBF-β) to form the active transcription factor complex known as the core binding factor (CBF).

The CBF complex binds to the CCAAT box, a specific DNA sequence found in the promoter regions of many genes. By binding to this sequence, the CBF complex can either activate or repress the transcription of target genes, depending on the context and the presence of other regulatory factors.

Mutations in the gene encoding CBF-A2 have been associated with several human diseases, including acute myeloid leukemia (AML) and multiple myeloma. In AML, mutations in the CBF-A2 gene can lead to the formation of abnormal CBF complexes that disrupt normal gene expression patterns and contribute to the development of leukemia.

Sp1 (Specificity Protein 1) transcription factor is a protein that binds to specific DNA sequences, known as GC boxes, in the promoter regions of many genes. It plays a crucial role in the regulation of gene expression by controlling the initiation of transcription. Sp1 recognizes and binds to the consensus sequence of GGGCGG upstream of the transcription start site, thereby recruiting other co-activators or co-repressors to modulate the rate of transcription. Sp1 is involved in various cellular processes, including cell growth, differentiation, and apoptosis, and its dysregulation has been implicated in several human diseases, such as cancer.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.

In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Telomeric Repeat Binding Protein 2 (TRF2) is a protein that binds to the telomeres, which are the repetitive DNA sequences found at the ends of chromosomes. TRF2 plays a crucial role in protecting the telomeres from being recognized as damaged or broken DNA, which could otherwise lead to chromosomal instability and cellular senescence or apoptosis.

TRF2 is a member of the shelterin complex, a group of proteins that bind to and protect telomeres. TRF2 specifically binds to double-stranded TTAGGG repeats in the telomeric DNA through its N-terminal Myb-like DNA binding domain. By binding to the telomeres, TRF2 helps to prevent the activation of the DNA damage response (DDR) pathway and the subsequent activation of p53-dependent cell cycle checkpoints or apoptosis.

TRF2 has also been shown to play a role in regulating the length of telomeres. It can inhibit the activity of telomerase, an enzyme that adds repetitive DNA sequences to the ends of chromosomes, thereby limiting the extension of telomeres. TRF2 can also promote the formation of t-loops, a higher-order structure in which the 3' overhang of the telomere invades the double-stranded telomeric DNA, forming a displacement loop (D-loop). This helps to protect the telomere from being recognized as a double-strand break and degraded by nucleases.

Mutations in TRF2 have been associated with several human diseases, including premature aging disorders such as dyskeratosis congenita and Hoyeraal-Hreidarsson syndrome, as well as cancer.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Transcription factors (TFs) are proteins that regulate the transcription of genetic information from DNA to RNA by binding to specific DNA sequences. They play a crucial role in controlling gene expression, which is the process by which information in genes is converted into a functional product, such as a protein.

TFII, on the other hand, refers to a general class of transcription factors that are involved in the initiation of RNA polymerase II-dependent transcription. These proteins are often referred to as "general transcription factors" because they are required for the transcription of most protein-coding genes in eukaryotic cells.

TFII factors help to assemble the preinitiation complex (PIC) at the promoter region of a gene, which is a group of proteins that includes RNA polymerase II and other cofactors necessary for transcription. Once the PIC is assembled, TFII factors help to recruit RNA polymerase II to the promoter and initiate transcription.

Some examples of TFII factors include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIIH. Each of these factors plays a specific role in the initiation of transcription, such as recognizing and binding to specific DNA sequences or modifying the chromatin structure around the promoter to make it more accessible to RNA polymerase II.

Core Binding Factor Alpha 1 Subunit, also known as CBF-A1 or RUNX1, is a protein that plays a crucial role in hematopoiesis, which is the process of blood cell development. It is a member of the core binding factor (CBF) complex, which regulates gene transcription and is essential for the differentiation and maturation of hematopoietic stem cells into mature blood cells.

The CBF complex consists of three subunits: CBF-A, CBF-B, and a histone deacetylase (HDAC). The CBF-A subunit can have several isoforms, including CBF-A1, which is encoded by the RUNX1 gene. Mutations in the RUNX1 gene have been associated with various hematological disorders, such as acute myeloid leukemia (AML), familial platelet disorder with propensity to develop AML, and thrombocytopenia with absent radii syndrome.

CBF-A1/RUNX1 functions as a transcription factor that binds to DNA at specific sequences called core binding factors, thereby regulating the expression of target genes involved in hematopoiesis. Proper regulation of these genes is essential for normal blood cell development and homeostasis.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

RNA Polymerase I is a type of enzyme that carries out the transcription of ribosomal RNA (rRNA) genes in eukaryotic cells. These enzymes are responsible for synthesizing the rRNA molecules, which are crucial components of ribosomes, the cellular structures where protein synthesis occurs. RNA Polymerase I is found in the nucleolus, a specialized region within the nucleus of eukaryotic cells, and it primarily transcribes the 5S, 18S, and 28S rRNA genes. The enzyme binds to the promoter regions of these genes and synthesizes the rRNA molecules by adding ribonucleotides in a template-directed manner, using DNA as a template. This process is essential for maintaining normal cellular function and for the production of proteins required for growth, development, and homeostasis.

Genetic enhancer elements are DNA sequences that increase the transcription of specific genes. They work by binding to regulatory proteins called transcription factors, which in turn recruit RNA polymerase II, the enzyme responsible for transcribing DNA into messenger RNA (mRNA). This results in the activation of gene transcription and increased production of the protein encoded by that gene.

Enhancer elements can be located upstream, downstream, or even within introns of the genes they regulate, and they can act over long distances along the DNA molecule. They are an important mechanism for controlling gene expression in a tissue-specific and developmental stage-specific manner, allowing for the precise regulation of gene activity during embryonic development and throughout adult life.

It's worth noting that genetic enhancer elements are often referred to simply as "enhancers," and they are distinct from other types of regulatory DNA sequences such as promoters, silencers, and insulators.

Transcription Factor AP-2 is a specific protein involved in the process of gene transcription. It belongs to a family of transcription factors known as Activating Enhancer-Binding Proteins (AP-2). These proteins regulate gene expression by binding to specific DNA sequences called enhancers, which are located near the genes they control.

AP-2 is composed of four subunits that form a homo- or heterodimer, which then binds to the consensus sequence 5'-GCCNNNGGC-3'. This sequence is typically found in the promoter regions of target genes. Once bound, AP-2 can either activate or repress gene transcription, depending on the context and the presence of cofactors.

AP-2 plays crucial roles during embryonic development, particularly in the formation of the nervous system, limbs, and face. It is also involved in cell cycle regulation, differentiation, and apoptosis (programmed cell death). Dysregulation of AP-2 has been implicated in several diseases, including various types of cancer.

Regulatory sequences in nucleic acid refer to specific DNA or RNA segments that control the spatial and temporal expression of genes without encoding proteins. They are crucial for the proper functioning of cells as they regulate various cellular processes such as transcription, translation, mRNA stability, and localization. Regulatory sequences can be found in both coding and non-coding regions of DNA or RNA.

Some common types of regulatory sequences in nucleic acid include:

1. Promoters: DNA sequences typically located upstream of the gene that provide a binding site for RNA polymerase and transcription factors to initiate transcription.
2. Enhancers: DNA sequences, often located at a distance from the gene, that enhance transcription by binding to specific transcription factors and increasing the recruitment of RNA polymerase.
3. Silencers: DNA sequences that repress transcription by binding to specific proteins that inhibit the recruitment of RNA polymerase or promote chromatin compaction.
4. Intron splice sites: Specific nucleotide sequences within introns (non-coding regions) that mark the boundaries between exons (coding regions) and are essential for correct splicing of pre-mRNA.
5. 5' untranslated regions (UTRs): Regions located at the 5' end of an mRNA molecule that contain regulatory elements affecting translation efficiency, stability, and localization.
6. 3' untranslated regions (UTRs): Regions located at the 3' end of an mRNA molecule that contain regulatory elements influencing translation termination, stability, and localization.
7. miRNA target sites: Specific sequences in mRNAs that bind to microRNAs (miRNAs) leading to translational repression or degradation of the target mRNA.

The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.

The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).

The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.

Repressor proteins are a type of regulatory protein in molecular biology that suppress the transcription of specific genes into messenger RNA (mRNA) by binding to DNA. They function as part of gene regulation processes, often working in conjunction with an operator region and a promoter region within the DNA molecule. Repressor proteins can be activated or deactivated by various signals, allowing for precise control over gene expression in response to changing cellular conditions.

There are two main types of repressor proteins:

1. DNA-binding repressors: These directly bind to specific DNA sequences (operator regions) near the target gene and prevent RNA polymerase from transcribing the gene into mRNA.
2. Allosteric repressors: These bind to effector molecules, which then cause a conformational change in the repressor protein, enabling it to bind to DNA and inhibit transcription.

Repressor proteins play crucial roles in various biological processes, such as development, metabolism, and stress response, by controlling gene expression patterns in cells.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

The nucleolus is a structure found within the nucleus of eukaryotic cells (cells that contain a true nucleus). It plays a central role in the production and assembly of ribosomes, which are complex molecular machines responsible for protein synthesis. The nucleolus is not a distinct organelle with a membrane surrounding it, but rather a condensed region within the nucleus where ribosomal biogenesis takes place.

The process of ribosome formation begins in the nucleolus with the transcription of ribosomal DNA (rDNA) genes into long precursor RNA molecules called rRNAs (ribosomal RNAs). Within the nucleolus, these rRNA molecules are cleaved, modified, and assembled together with ribosomal proteins to form small and large ribosomal subunits. Once formed, these subunits are transported through the nuclear pores to the cytoplasm, where they come together to form functional ribosomes that can engage in protein synthesis.

In addition to its role in ribosome biogenesis, the nucleolus has been implicated in other cellular processes such as stress response, cell cycle regulation, and aging. Changes in nucleolar structure and function have been associated with various diseases, including cancer and neurodegenerative disorders.

HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.

HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.

It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.

Prostatic secretory proteins are a group of proteins that are produced and secreted by the prostate gland, which is a small gland that is part of the male reproductive system. These proteins play an important role in maintaining the health and function of the reproductive system.

One of the most well-known prostatic secretory proteins is prostate-specific antigen (PSA), which is often used as a biomarker for the early detection and monitoring of prostate cancer. PSA is a protein that is produced by the cells in the prostate gland and is normally found in low levels in the blood. However, when the prostate gland becomes enlarged or cancerous, the levels of PSA in the blood can increase, making it possible to detect these conditions through a simple blood test.

Other prostatic secretory proteins include prostate-specific acid phosphatase (PSAP), prostatein, and prolactin-inducible protein (PIP). These proteins are also produced by the prostate gland and have various functions, such as helping to liquefy semen and protecting sperm from the immune system.

It is important to note that while these proteins can provide valuable information about the health of the prostate gland, they are not foolproof indicators of disease. Other factors, such as age, inflammation, and benign prostatic hyperplasia (BPH), can also affect the levels of these proteins in the blood. Therefore, it is important to consult with a healthcare professional for proper interpretation and follow-up care.

Nuclear factor 90 proteins (NF-90) are a family of ubiquitously expressed nuclear factors that play important roles in regulating gene expression. They were originally discovered as proteins that bind to the IL-6 response element in the promoter region of the acute phase genes. NF-90 proteins have since been shown to be involved in various cellular processes, including transcriptional regulation, RNA processing, and translation.

NF-90 proteins are composed of two subunits, NF-90A and NF-90B, which form a heterodimer that binds to DNA and RNA. They have multiple functional domains, including an N-terminal double-stranded RNA binding domain (dsRBD), a central dimerization domain, and a C-terminal glycine-rich region involved in protein-protein interactions.

NF-90 proteins are known to interact with various transcription factors, chromatin modifiers, and RNA-binding proteins, suggesting that they function as adaptors or scaffolds in the assembly of large protein complexes involved in gene regulation. They have been shown to regulate the expression of genes involved in inflammation, immune response, cell cycle, apoptosis, and stress response.

In addition to their role in transcriptional regulation, NF-90 proteins also play important roles in RNA metabolism. They bind to double-stranded RNA (dsRNA) and regulate the stability and translation of mRNAs encoding cytokines, growth factors, and other regulatory molecules. NF-90 proteins have been shown to interact with microRNAs (miRNAs), small non-coding RNAs that regulate gene expression by binding to target mRNAs, and modulate their activity.

Overall, NF-90 proteins are important regulators of gene expression at multiple levels, including transcriptional regulation, RNA processing, and translation. Dysregulation of NF-90 function has been implicated in various human diseases, including cancer, inflammation, and neurodegenerative disorders.

The Nucleolus Organizer Region (NOR) is a specific region within the chromosomes, primarily in the short arm of the acrocentric chromosomes (chromosomes 13, 14, 15, 21, and 22). It consists of clusters of repetitive DNA sequences that encode ribosomal RNA (rRNA) genes. During interphase, these regions form the nucleolus, a distinct structure within the nucleus where rRNA transcription, processing, and ribosome assembly occur. The number of NORs in an individual can vary, which has implications in certain genetic conditions and aging processes.

Ribosomal RNA (rRNA) is a type of RNA molecule that is a key component of ribosomes, which are the cellular structures where protein synthesis occurs in cells. In ribosomes, rRNA plays a crucial role in the process of translation, where genetic information from messenger RNA (mRNA) is translated into proteins.

Ribosomal RNA is synthesized in the nucleus and then transported to the cytoplasm, where it assembles with ribosomal proteins to form ribosomes. Within the ribosome, rRNA provides a structural framework for the assembly of the ribosome and also plays an active role in catalyzing the formation of peptide bonds between amino acids during protein synthesis.

There are several different types of rRNA molecules, including 5S, 5.8S, 18S, and 28S rRNA, which vary in size and function. These rRNA molecules are highly conserved across different species, indicating their essential role in protein synthesis and cellular function.

Lymphoid Enhancer-Binding Factor 1 (LEF1) is a protein that functions as a transcription factor, playing a crucial role in the Wnt signaling pathway. It is involved in the regulation of gene expression, particularly during embryonic development and immune system function. LEF1 helps control the differentiation and proliferation of certain cells, including B and T lymphocytes, which are essential for adaptive immunity. Mutations in the LEF1 gene have been associated with various human diseases, such as cancer and immunodeficiency disorders.

Deoxyribonuclease I (DNase I) is an enzyme that cleaves the phosphodiester bonds in the DNA molecule, breaking it down into smaller pieces. It is also known as DNase A or bovine pancreatic deoxyribonuclease. This enzyme specifically hydrolyzes the internucleotide linkages of DNA by cleaving the phosphodiester bond between the 3'-hydroxyl group of one deoxyribose sugar and the phosphate group of another, leaving 3'-phosphomononucleotides as products.

DNase I plays a crucial role in various biological processes, including DNA degradation during apoptosis (programmed cell death), DNA repair, and host defense against pathogens by breaking down extracellular DNA from invading microorganisms or damaged cells. It is widely used in molecular biology research for applications such as DNA isolation, removing contaminating DNA from RNA samples, and generating defined DNA fragments for cloning purposes. DNase I can be found in various sources, including bovine pancreas, human tears, and bacterial cultures.

An oligonucleotide probe is a short, single-stranded DNA or RNA molecule that contains a specific sequence of nucleotides designed to hybridize with a complementary sequence in a target nucleic acid (DNA or RNA). These probes are typically 15-50 nucleotides long and are used in various molecular biology techniques, such as polymerase chain reaction (PCR), DNA sequencing, microarray analysis, and blotting methods.

Oligonucleotide probes can be labeled with various reporter molecules, like fluorescent dyes or radioactive isotopes, to enable the detection of hybridized targets. The high specificity of oligonucleotide probes allows for the precise identification and quantification of target nucleic acids in complex biological samples, making them valuable tools in diagnostic, research, and forensic applications.

An Electrophoretic Mobility Shift Assay (EMSA) is a laboratory technique used to detect and analyze protein-DNA interactions. In this assay, a mixture of proteins and fluorescently or radioactively labeled DNA probes are loaded onto a native polyacrylamide gel matrix and subjected to an electric field. The negatively charged DNA probe migrates towards the positive electrode, and the rate of migration (mobility) is dependent on the size and charge of the molecule. When a protein binds to the DNA probe, it forms a complex that has a different size and/or charge than the unbound probe, resulting in a shift in its mobility on the gel.

The EMSA can be used to identify specific protein-DNA interactions, determine the binding affinity of proteins for specific DNA sequences, and investigate the effects of mutations or post-translational modifications on protein-DNA interactions. The technique is widely used in molecular biology research, including studies of gene regulation, DNA damage repair, and epigenetic modifications.

In summary, Electrophoretic Mobility Shift Assay (EMSA) is a laboratory technique that detects and analyzes protein-DNA interactions by subjecting a mixture of proteins and labeled DNA probes to an electric field in a native polyacrylamide gel matrix. The binding of proteins to the DNA probe results in a shift in its mobility on the gel, allowing for the detection and analysis of specific protein-DNA interactions.

Gene expression regulation in plants refers to the processes that control the production of proteins and RNA from the genes present in the plant's DNA. This regulation is crucial for normal growth, development, and response to environmental stimuli in plants. It can occur at various levels, including transcription (the first step in gene expression, where the DNA sequence is copied into RNA), RNA processing (such as alternative splicing, which generates different mRNA molecules from a single gene), translation (where the information in the mRNA is used to produce a protein), and post-translational modification (where proteins are chemically modified after they have been synthesized).

In plants, gene expression regulation can be influenced by various factors such as hormones, light, temperature, and stress. Plants use complex networks of transcription factors, chromatin remodeling complexes, and small RNAs to regulate gene expression in response to these signals. Understanding the mechanisms of gene expression regulation in plants is important for basic research, as well as for developing crops with improved traits such as increased yield, stress tolerance, and disease resistance.

Smooth muscle myosin is a type of motor protein that is responsible for the contraction and relaxation of smooth muscles, which are found in various organs such as the bladder, blood vessels, and digestive tract. Smooth muscle myosin is composed of two heavy chains and four light chains, forming a hexameric structure. The heavy chains have an N-terminal head domain that contains the ATPase activity and a C-terminal tail domain that mediates filament assembly.

The smooth muscle myosin molecule has several unique features compared to other types of myosins, such as skeletal or cardiac myosin. For example, smooth muscle myosin has a longer lever arm, which allows for greater force generation during contraction. Additionally, the regulatory mechanism of smooth muscle myosin is different from that of skeletal or cardiac myosin. In smooth muscles, the contractile activity is regulated by phosphorylation of the light chains, which is mediated by a specific kinase called myosin light chain kinase (MLCK).

Overall, the proper regulation and function of smooth muscle myosin are critical for maintaining normal physiological functions in various organs. Dysregulation or mutations in smooth muscle myosin can lead to several diseases, such as hypertension, atherosclerosis, and gastrointestinal motility disorders.

A telomere is a region of repetitive DNA sequences found at the end of chromosomes, which protects the genetic data from damage and degradation during cell division. Telomeres naturally shorten as cells divide, and when they become too short, the cell can no longer divide and becomes senescent or dies. This natural process is associated with aging and various age-related diseases. The length of telomeres can also be influenced by various genetic and environmental factors, including stress, diet, and lifestyle.

A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.

The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.

The main components of a two-hybrid system include:

1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)

The two-hybrid system technique has several advantages, including:

1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis

However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Ribosomal DNA (rDNA) refers to the specific regions of DNA in a cell that contain the genes for ribosomal RNA (rRNA). Ribosomes are complex structures composed of proteins and rRNA, which play a crucial role in protein synthesis by translating messenger RNA (mRNA) into proteins.

In humans, there are four types of rRNA molecules: 18S, 5.8S, 28S, and 5S. These rRNAs are encoded by multiple copies of rDNA genes that are organized in clusters on specific chromosomes. In humans, the majority of rDNA genes are located on the short arms of acrocentric chromosomes 13, 14, 15, 21, and 22.

Each cluster of rDNA genes contains both transcribed and non-transcribed spacer regions. The transcribed regions contain the genes for the four types of rRNA, while the non-transcribed spacers contain regulatory elements that control the transcription of the rRNA genes.

The number of rDNA copies varies between species and even within individuals of the same species. The copy number can also change during development and in response to environmental factors. Variations in rDNA copy number have been associated with various diseases, including cancer and neurological disorders.

Basic-leucine zipper (bZIP) transcription factors are a family of transcriptional regulatory proteins characterized by the presence of a basic region and a leucine zipper motif. The basic region, which is rich in basic amino acids such as lysine and arginine, is responsible for DNA binding, while the leucine zipper motif mediates protein-protein interactions and dimerization.

BZIP transcription factors play important roles in various cellular processes, including gene expression regulation, cell growth, differentiation, and stress response. They bind to specific DNA sequences called AP-1 sites, which are often found in the promoter regions of target genes. BZIP transcription factors can form homodimers or heterodimers with other bZIP proteins, allowing for combinatorial control of gene expression.

Examples of bZIP transcription factors include c-Jun, c-Fos, ATF (activating transcription factor), and CREB (cAMP response element-binding protein). Dysregulation of bZIP transcription factors has been implicated in various diseases, including cancer, inflammation, and neurodegenerative disorders.

Heterogeneous Nuclear Ribonucleoprotein D (hnRNP D) is a member of the family of heterogeneous nuclear ribonucleoproteins (hnRNPs). These proteins are involved in various aspects of RNA metabolism, such as processing, transport, and stability. Specifically, hnRNP D, also known as AU-rich element RNA-binding protein 1 (AUF1), is a single-stranded nucleic acid-binding protein that binds to specific sequences in the 3' untranslated region of certain mRNAs, including those that are involved in inflammatory responses and oncogenesis. By binding to these sequences, hnRNP D can regulate the stability, translation, and localization of target mRNAs. It is a shuttling protein that can be found both in the nucleus and cytoplasm. Mutations in the gene encoding hnRNP D have been associated with several human diseases, including cancer and neurological disorders.

DNA footprinting is a laboratory technique used to identify specific DNA-protein interactions and map the binding sites of proteins on a DNA molecule. This technique involves the use of enzymes or chemicals that can cleave the DNA strand, but are prevented from doing so when a protein is bound to the DNA. By comparing the pattern of cuts in the presence and absence of the protein, researchers can identify the regions of the DNA where the protein binds.

The process typically involves treating the DNA-protein complex with a chemical or enzymatic agent that cleaves the DNA at specific sequences or sites. After the reaction is stopped, the DNA is separated into single strands and analyzed using techniques such as gel electrophoresis to visualize the pattern of cuts. The regions of the DNA where protein binding has occurred are protected from cleavage and appear as gaps or "footprints" in the pattern of cuts.

DNA footprinting is a valuable tool for studying gene regulation, as it can provide insights into how proteins interact with specific DNA sequences to control gene expression. It can also be used to study protein-DNA interactions involved in processes such as DNA replication, repair, and recombination.

Tankyrases are a group of proteins that belong to the poly (ADP-ribose) polymerase (PARP) family, specifically PARP5a and PARP5b. They play roles in various cellular processes such as telomere maintenance, Wnt signaling pathway regulation, and protein trafficking. Tankyrases add poly(ADP-ribose) chains to their target proteins, leading to changes in their function, localization, or stability. Dysregulation of tankyrases has been implicated in several diseases, including cancer.

Telomere-binding proteins are specialized proteins that bind to the telomeres, which are the repetitive DNA sequences found at the ends of chromosomes. These proteins play a crucial role in protecting the structural integrity and stability of chromosomes by preventing the degradation of telomeres during cell division and preventing the chromosomes from being recognized as damaged or broken.

One of the most well-known telomere-binding proteins is called TRF2 (telomeric repeat-binding factor 2), which helps to maintain the structure of the telomere "T-loop" and prevent the activation of DNA repair mechanisms that can lead to chromosomal instability. Another important telomere-binding protein is called POT1 (protection of telomeres 1), which specifically binds to the single-stranded overhang of the telomere and helps to regulate the activity of telomerase, an enzyme that adds DNA repeats to the ends of chromosomes during cell division.

Mutations in telomere-binding proteins have been linked to a variety of human diseases, including premature aging disorders, cancer, and bone marrow failure syndromes. Therefore, understanding the function and regulation of these proteins is an important area of research in molecular biology and genetics.

"Competitive binding" is a term used in pharmacology and biochemistry to describe the behavior of two or more molecules (ligands) competing for the same binding site on a target protein or receptor. In this context, "binding" refers to the physical interaction between a ligand and its target.

When a ligand binds to a receptor, it can alter the receptor's function, either activating or inhibiting it. If multiple ligands compete for the same binding site, they will compete to bind to the receptor. The ability of each ligand to bind to the receptor is influenced by its affinity for the receptor, which is a measure of how strongly and specifically the ligand binds to the receptor.

In competitive binding, if one ligand is present in high concentrations, it can prevent other ligands with lower affinity from binding to the receptor. This is because the higher-affinity ligand will have a greater probability of occupying the binding site and blocking access to the other ligands. The competition between ligands can be described mathematically using equations such as the Langmuir isotherm, which describes the relationship between the concentration of ligand and the fraction of receptors that are occupied by the ligand.

Competitive binding is an important concept in drug development, as it can be used to predict how different drugs will interact with their targets and how they may affect each other's activity. By understanding the competitive binding properties of a drug, researchers can optimize its dosage and delivery to maximize its therapeutic effect while minimizing unwanted side effects.

Immunoglobulin J (JOINING) recombination signal sequence-binding protein, also known as RAG1 or RAG-1, is a protein that plays a critical role in the adaptive immune system. It is a component of the RAG complex, which also includes RAG2 and several other proteins.

The RAG complex is responsible for initiating the V(D)J recombination process, during which the variable regions of immunoglobulin (antibody) genes and T-cell receptor genes are assembled from gene segments called variable (V), diversity (D), and joining (J) segments. This process generates a diverse repertoire of antigen receptors that enable the immune system to recognize and respond to a wide range of pathogens.

RAG1 is an endonuclease that recognizes and cleaves specific sequences in the DNA called recombination signal sequences (RSSs) that flank the V, D, and J segments. Cleavage of these RSSs by RAG1 and RAG2 creates double-stranded breaks in the DNA, which are then processed by other proteins to form functional antigen receptor genes through a process called non-homologous end joining (NHEJ).

Therefore, Immunoglobulin J recombination signal sequence-binding protein is a crucial player in the adaptive immune system's ability to generate a diverse repertoire of antigen receptors and respond effectively to pathogens.

Oligodeoxyribonucleotides (ODNs) are relatively short, synthetic single-stranded DNA molecules. They typically contain 15 to 30 nucleotides, but can range from 2 to several hundred nucleotides in length. ODNs are often used as tools in molecular biology research for various applications such as:

1. Nucleic acid detection and quantification (e.g., real-time PCR)
2. Gene regulation (antisense, RNA interference)
3. Gene editing (CRISPR-Cas systems)
4. Vaccine development
5. Diagnostic purposes

Due to their specificity and affinity towards complementary DNA or RNA sequences, ODNs can be designed to target a particular gene or sequence of interest. This makes them valuable tools in understanding gene function, regulation, and interaction with other molecules within the cell.

RNA-binding proteins (RBPs) are a class of proteins that selectively interact with RNA molecules to form ribonucleoprotein complexes. These proteins play crucial roles in the post-transcriptional regulation of gene expression, including pre-mRNA processing, mRNA stability, transport, localization, and translation. RBPs recognize specific RNA sequences or structures through their modular RNA-binding domains, which can be highly degenerate and allow for the recognition of a wide range of RNA targets. The interaction between RBPs and RNA is often dynamic and can be regulated by various post-translational modifications of the proteins or by environmental stimuli, allowing for fine-tuning of gene expression in response to changing cellular needs. Dysregulation of RBP function has been implicated in various human diseases, including neurological disorders and cancer.

High mobility group proteins (HMG proteins) are a family of nuclear proteins that are characterized by their ability to bind to DNA and influence its structure and function. They are named "high mobility" because of their rapid movement in gel electrophoresis. HMG proteins are involved in various nuclear processes, including chromatin remodeling, transcription regulation, and DNA repair.

There are three main classes of HMG proteins: HMGA, HMGB, and HMGN. Each class has distinct structural features and functions. For example, HMGA proteins have a unique "AT-hook" domain that allows them to bind to the minor groove of AT-rich DNA sequences, while HMGB proteins have two "HMG-box" domains that enable them to bend and unwind DNA.

HMG proteins play important roles in many physiological and pathological processes, such as embryonic development, inflammation, and cancer. Dysregulation of HMG protein function has been implicated in various diseases, including neurodegenerative disorders, diabetes, and cancer. Therefore, understanding the structure, function, and regulation of HMG proteins is crucial for developing new therapeutic strategies for these diseases.

"Vaccinium" is not a medical term, but a scientific name for a genus of plants in the family Ericaceae. It includes several species of shrubs that produce berries, such as blueberries, cranberries, and huckleberries. While these fruits have nutritional and potential medicinal benefits, "Vaccinium" itself does not have a medical definition.

Sequence homology in nucleic acids refers to the similarity or identity between the nucleotide sequences of two or more DNA or RNA molecules. It is often used as a measure of biological relationship between genes, organisms, or populations. High sequence homology suggests a recent common ancestry or functional constraint, while low sequence homology may indicate a more distant relationship or different functions.

Nucleic acid sequence homology can be determined by various methods such as pairwise alignment, multiple sequence alignment, and statistical analysis. The degree of homology is typically expressed as a percentage of identical or similar nucleotides in a given window of comparison.

It's important to note that the interpretation of sequence homology depends on the biological context and the evolutionary distance between the sequences compared. Therefore, functional and experimental validation is often necessary to confirm the significance of sequence homology.

"Response elements" is a term used in molecular biology, particularly in the study of gene regulation. Response elements are specific DNA sequences that can bind to transcription factors, which are proteins that regulate gene expression. When a transcription factor binds to a response element, it can either activate or repress the transcription of the nearby gene.

Response elements are often found in the promoter region of genes and are typically short, conserved sequences that can be recognized by specific transcription factors. The binding of a transcription factor to a response element can lead to changes in chromatin structure, recruitment of co-activators or co-repressors, and ultimately, the regulation of gene expression.

Response elements are important for many biological processes, including development, differentiation, and response to environmental stimuli such as hormones, growth factors, and stress. The specificity of transcription factor binding to response elements allows for precise control of gene expression in response to changing conditions within the cell or organism.

"Vaccinium vitis-idaea" is the scientific name for a species of shrub that produces edible berries known as lingonberries or cowberries. While the plant itself is not a medical term, its berries have been used in traditional medicine for their potential health benefits. However, it's important to note that these benefits have not been extensively studied and are not widely recognized in modern medicine.

The berries of Vaccinium vitis-idaea contain various compounds such as polyphenols, anthocyanins, and vitamin C, which may have antioxidant properties. Some studies suggest that consuming these berries may help protect against oxidative stress, inflammation, and certain chronic diseases. However, more research is needed to confirm these potential health benefits and establish recommended dosages.

Therefore, while Vaccinium vitis-idaea has been used in traditional medicine, it does not have a specific medical definition as a treatment or cure for any disease or condition.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

'Arabidopsis' is a genus of small flowering plants that are part of the mustard family (Brassicaceae). The most commonly studied species within this genus is 'Arabidopsis thaliana', which is often used as a model organism in plant biology and genetics research. This plant is native to Eurasia and Africa, and it has a small genome that has been fully sequenced. It is known for its short life cycle, self-fertilization, and ease of growth, making it an ideal subject for studying various aspects of plant biology, including development, metabolism, and response to environmental stresses.

Basic Helix-Loop-Helix (bHLH) Leucine Zipper Transcription Factors are a type of transcription factors that share a common structural feature consisting of two amphipathic α-helices connected by a loop. The bHLH domain is involved in DNA binding and dimerization, while the leucine zipper motif mediates further stabilization of the dimer. These transcription factors play crucial roles in various biological processes such as cell fate determination, proliferation, differentiation, and apoptosis. They bind to specific DNA sequences called E-box motifs, which are CANNTG nucleotide sequences, often found in the promoter or enhancer regions of their target genes.

Acclimatization is the process by which an individual organism adjusts to a change in its environment, enabling it to maintain its normal physiological functions and thus survive and reproduce. In the context of medicine, acclimatization often refers to the body's adaptation to changes in temperature, altitude, or other environmental factors that can affect health.

For example, when a person moves from a low-altitude area to a high-altitude area, their body may undergo several physiological changes to adapt to the reduced availability of oxygen at higher altitudes. These changes may include increased breathing rate and depth, increased heart rate, and altered blood chemistry, among others. This process of acclimatization can take several days or even weeks, depending on the individual and the degree of environmental change.

Similarly, when a person moves from a cold climate to a hot climate, their body may adjust by increasing its sweat production and reducing its heat production, in order to maintain a stable body temperature. This process of acclimatization can help prevent heat-related illnesses such as heat exhaustion and heat stroke.

Overall, acclimatization is an important physiological process that allows organisms to adapt to changing environments and maintain their health and well-being.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

'Tumor cells, cultured' refers to the process of removing cancerous cells from a tumor and growing them in controlled laboratory conditions. This is typically done by isolating the tumor cells from a patient's tissue sample, then placing them in a nutrient-rich environment that promotes their growth and multiplication.

The resulting cultured tumor cells can be used for various research purposes, including the study of cancer biology, drug development, and toxicity testing. They provide a valuable tool for researchers to better understand the behavior and characteristics of cancer cells outside of the human body, which can lead to the development of more effective cancer treatments.

It is important to note that cultured tumor cells may not always behave exactly the same way as they do in the human body, so findings from cell culture studies must be validated through further research, such as animal models or clinical trials.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Human chromosome pair 16 consists of two rod-shaped structures present in the nucleus of each cell in the human body. Each chromosome is made up of DNA tightly coiled around histone proteins, forming a complex structure called a chromatin.

Chromosomes come in pairs, with one chromosome inherited from each parent. Chromosome pair 16 contains two homologous chromosomes, which are similar in size, shape, and genetic content but may have slight variations due to differences in the DNA sequences inherited from each parent.

Chromosome pair 16 is one of the 22 autosomal pairs, meaning it contains non-sex chromosomes that are present in both males and females. Chromosome 16 is a medium-sized chromosome, and it contains around 2,800 genes that provide instructions for making proteins and regulating various cellular processes.

Abnormalities in chromosome pair 16 can lead to genetic disorders such as chronic myeloid leukemia, some forms of mental retardation, and other developmental abnormalities.

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

"Freezing" is a term used in the medical field to describe a phenomenon that can occur in certain neurological conditions, most notably in Parkinson's disease. It refers to a sudden and temporary inability to move or initiate movement, often triggered by environmental factors such as narrow spaces, turning, or approaching a destination. This can increase the risk of falls and make daily activities challenging for affected individuals.

Freezing is also known as "freezing of gait" (FOG) when it specifically affects a person's ability to walk. During FOG episodes, the person may feel like their feet are glued to the ground, making it difficult to take steps forward. This can be very distressing and debilitating for those affected.

It is important to note that "freezing" has different meanings in different medical contexts, such as in the field of orthopedics, where it may refer to a loss of joint motion due to stiffness or inflammation. Always consult with a healthcare professional for accurate information tailored to your specific situation.

A consensus sequence in genetics refers to the most common nucleotide (DNA or RNA) or amino acid at each position in a multiple sequence alignment. It is derived by comparing and analyzing several sequences of the same gene or protein from different individuals or organisms. The consensus sequence provides a general pattern or motif that is shared among these sequences and can be useful in identifying functional regions, conserved domains, or evolutionary relationships. However, it's important to note that not every sequence will exactly match the consensus sequence, as variations can occur naturally due to mutations or genetic differences among individuals.

Regulator genes are a type of gene that regulates the activity of other genes in an organism. They do not code for a specific protein product but instead control the expression of other genes by producing regulatory proteins such as transcription factors, repressors, or enhancers. These regulatory proteins bind to specific DNA sequences near the target genes and either promote or inhibit their transcription into mRNA. This allows regulator genes to play a crucial role in coordinating complex biological processes, including development, differentiation, metabolism, and response to environmental stimuli.

There are several types of regulator genes, including:

1. Constitutive regulators: These genes are always active and produce regulatory proteins that control the expression of other genes in a consistent manner.
2. Inducible regulators: These genes respond to specific signals or environmental stimuli by producing regulatory proteins that modulate the expression of target genes.
3. Negative regulators: These genes produce repressor proteins that bind to DNA and inhibit the transcription of target genes, thereby reducing their expression.
4. Positive regulators: These genes produce activator proteins that bind to DNA and promote the transcription of target genes, thereby increasing their expression.
5. Master regulators: These genes control the expression of multiple downstream target genes involved in specific biological processes or developmental pathways.

Regulator genes are essential for maintaining proper gene expression patterns and ensuring normal cellular function. Mutations in regulator genes can lead to various diseases, including cancer, developmental disorders, and metabolic dysfunctions.

A chromosome inversion is a genetic rearrangement where a segment of a chromosome has been reversed end to end, so that its order of genes is opposite to the original. This means that the gene sequence on the segment of the chromosome has been inverted.

In an inversion, the chromosome breaks in two places, and the segment between the breaks rotates 180 degrees before reattaching. This results in a portion of the chromosome being inverted, or turned upside down, relative to the rest of the chromosome.

Chromosome inversions can be either paracentric or pericentric. Paracentric inversions involve a segment that does not include the centromere (the central constriction point of the chromosome), while pericentric inversions involve a segment that includes the centromere.

Inversions can have various effects on an individual's phenotype, depending on whether the inversion involves genes and if so, how those genes are affected by the inversion. In some cases, inversions may have no noticeable effect, while in others they may cause genetic disorders or predispose an individual to certain health conditions.

A sequence deletion in a genetic context refers to the removal or absence of one or more nucleotides (the building blocks of DNA or RNA) from a specific region in a DNA or RNA molecule. This type of mutation can lead to the loss of genetic information, potentially resulting in changes in the function or expression of a gene. If the deletion involves a critical portion of the gene, it can cause diseases, depending on the role of that gene in the body. The size of the deleted sequence can vary, ranging from a single nucleotide to a large segment of DNA.

"Cold temperature" is a relative term and its definition can vary depending on the context. In general, it refers to temperatures that are lower than those normally experienced or preferred by humans and other warm-blooded animals. In a medical context, cold temperature is often defined as an environmental temperature that is below 16°C (60.8°F).

Exposure to cold temperatures can have various physiological effects on the human body, such as vasoconstriction of blood vessels near the skin surface, increased heart rate and metabolic rate, and shivering, which helps to generate heat and maintain body temperature. Prolonged exposure to extreme cold temperatures can lead to hypothermia, a potentially life-threatening condition characterized by a drop in core body temperature below 35°C (95°F).

It's worth noting that some people may have different sensitivities to cold temperatures due to factors such as age, health status, and certain medical conditions. For example, older adults, young children, and individuals with circulatory or neurological disorders may be more susceptible to the effects of cold temperatures.

Saccharomyces cerevisiae proteins are the proteins that are produced by the budding yeast, Saccharomyces cerevisiae. This organism is a single-celled eukaryote that has been widely used as a model organism in scientific research for many years due to its relatively simple genetic makeup and its similarity to higher eukaryotic cells.

The genome of Saccharomyces cerevisiae has been fully sequenced, and it is estimated to contain approximately 6,000 genes that encode proteins. These proteins play a wide variety of roles in the cell, including catalyzing metabolic reactions, regulating gene expression, maintaining the structure of the cell, and responding to environmental stimuli.

Many Saccharomyces cerevisiae proteins have human homologs and are involved in similar biological processes, making this organism a valuable tool for studying human disease. For example, many of the proteins involved in DNA replication, repair, and recombination in yeast have human counterparts that are associated with cancer and other diseases. By studying these proteins in yeast, researchers can gain insights into their function and regulation in humans, which may lead to new treatments for disease.

Repetitive sequences in nucleic acid refer to repeated stretches of DNA or RNA nucleotide bases that are present in a genome. These sequences can vary in length and can be arranged in different patterns such as direct repeats, inverted repeats, or tandem repeats. In some cases, these repetitive sequences do not code for proteins and are often found in non-coding regions of the genome. They can play a role in genetic instability, regulation of gene expression, and evolutionary processes. However, certain types of repeat expansions have been associated with various neurodegenerative disorders and other human diseases.

DNA primers are short single-stranded DNA molecules that serve as a starting point for DNA synthesis. They are typically used in laboratory techniques such as the polymerase chain reaction (PCR) and DNA sequencing. The primer binds to a complementary sequence on the DNA template through base pairing, providing a free 3'-hydroxyl group for the DNA polymerase enzyme to add nucleotides and synthesize a new strand of DNA. This allows for specific and targeted amplification or analysis of a particular region of interest within a larger DNA molecule.

Upstream stimulatory factors (USF) are a group of transcription factors that bind to the promoter or enhancer regions of genes and regulate their expression. They are called "upstream" because they bind to the DNA upstream of the gene's transcription start site. USFs are widely expressed in many tissues and play important roles in various cellular processes, including cell growth, differentiation, and metabolism.

There are two main members of the USF family, USF-1 and USF-2, which are encoded by separate genes but share a high degree of sequence similarity. Both USF proteins contain a conserved basic helix-loop-helix (bHLH) domain that mediates DNA binding and a conserved adjacent leucine zipper motif that facilitates protein dimerization. USFs can form homodimers or heterodimers with each other, as well as with other bHLH proteins, to regulate gene expression.

USFs have been shown to bind to and activate the transcription of a wide range of genes involved in various cellular processes, such as glycolysis, gluconeogenesis, lipid metabolism, and DNA repair. Dysregulation of USF activity has been implicated in several human diseases, including cancer, diabetes, and neurodegenerative disorders. Therefore, understanding the mechanisms of USF-mediated gene regulation may provide insights into the pathophysiology of these diseases and lead to the development of novel therapeutic strategies.

Homeodomain proteins are a group of transcription factors that play crucial roles in the development and differentiation of cells in animals and plants. They are characterized by the presence of a highly conserved DNA-binding domain called the homeodomain, which is typically about 60 amino acids long. The homeodomain consists of three helices, with the third helix responsible for recognizing and binding to specific DNA sequences.

Homeodomain proteins are involved in regulating gene expression during embryonic development, tissue maintenance, and organismal growth. They can act as activators or repressors of transcription, depending on the context and the presence of cofactors. Mutations in homeodomain proteins have been associated with various human diseases, including cancer, congenital abnormalities, and neurological disorders.

Some examples of homeodomain proteins include PAX6, which is essential for eye development, HOX genes, which are involved in body patterning, and NANOG, which plays a role in maintaining pluripotency in stem cells.

E-box elements are specific DNA sequences found in the promoter regions of many genes, particularly those involved in controlling the circadian rhythm (the biological "body clock") in mammals. These sequences are binding sites for various transcription factors that regulate gene expression. The E-box element is typically a 12-base pair sequence (5'-CACGTG-3') that can form a stem-loop structure, making it an ideal recognition site for helix-loop-helix (HLH) transcription factors.

There are two types of E-box elements: the canonical E-box (also called the ' evening element' or EE), and the non-canonical E-box (also known as the ' dawn element' or DE). The canonical E-box has a palindromic sequence (5'-CACGTG-3'), while the non-canonical E-box contains a single copy of the core motif (5'-CACGT-3').

The most well-known transcription factors that bind to E-box elements are CLOCK and BMAL1, which form heterodimers through their HLH domains. These heterodimers bind to the canonical E-box element in the promoter regions of target genes, leading to the recruitment of other coactivators and histone acetyltransferases that ultimately result in transcriptional activation.

The activity of CLOCK-BMAL1 complexes follows a circadian rhythm, with peak binding and gene expression occurring during the early night (evening) phase. In contrast, non-canonical E-box elements are bound by other transcription factors such as PERIOD (PER) proteins, which accumulate and repress CLOCK-BMAL1-mediated transcription during the late night to early morning (dawn) phase.

Overall, E-box elements play a crucial role in regulating circadian rhythm-controlled gene expression, contributing to various physiological processes such as sleep-wake cycles, metabolism, and hormone secretion.

Fungal proteins are a type of protein that is specifically produced and present in fungi, which are a group of eukaryotic organisms that include microorganisms such as yeasts and molds. These proteins play various roles in the growth, development, and survival of fungi. They can be involved in the structure and function of fungal cells, metabolism, pathogenesis, and other cellular processes. Some fungal proteins can also have important implications for human health, both in terms of their potential use as therapeutic targets and as allergens or toxins that can cause disease.

Fungal proteins can be classified into different categories based on their functions, such as enzymes, structural proteins, signaling proteins, and toxins. Enzymes are proteins that catalyze chemical reactions in fungal cells, while structural proteins provide support and protection for the cell. Signaling proteins are involved in communication between cells and regulation of various cellular processes, and toxins are proteins that can cause harm to other organisms, including humans.

Understanding the structure and function of fungal proteins is important for developing new treatments for fungal infections, as well as for understanding the basic biology of fungi. Research on fungal proteins has led to the development of several antifungal drugs that target specific fungal enzymes or other proteins, providing effective treatment options for a range of fungal diseases. Additionally, further study of fungal proteins may reveal new targets for drug development and help improve our ability to diagnose and treat fungal infections.

Brantjes H, Roose J, van De Wetering M, Clevers H (April 2001). "All Tcf HMG box transcription factors interact with Groucho- ... It's a member of T cell factor/lymphoid enhancer factor (TCF/LEF) family. Lymphoid enhancer-binding factor-1 (LEF1) is a 48-kD ... with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor ... with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor ...
The TATA-binding protein (TBP) is a general transcription factor that binds specifically to a DNA sequence called the TATA box ... Binding of TFIID to the TATA box in the promoter region of the gene initiates the recruitment of other factors required for RNA ... "Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding". J. Biol. Chem ... this region binds to the TATA box and interacts with transcription factors and regulatory proteins . By contrast, the N- ...
Similar to TBP, TBPL2 can bind to the TATA box. It interacts with other general transcription factors such as TFIIA and TFIIB ... a TATA-box-binding protein-related factor, is vertebrate-specific and widely expressed". Proceedings of the National Academy of ... TATA-box binding protein like 2 is a protein that in humans is encoded by the TBPL2 gene. The TBPL2 protein is also known as ... "Entrez Gene: TATA-box binding protein like 2". Retrieved 2018-01-31. Persengiev SP, Zhu X, Dixit BL, Maston GA, Kittler EL, ...
L'Etoile ND, Fahnestock ML, Shen Y, Aebersold R, Berk AJ (Apr 1994). "Human transcription factor IIIC box B binding subunit". ... General transcription factor 3C polypeptide 1 is a protein that in humans is encoded by the GTF3C1 gene. GTF3C1 has been shown ... "Entrez Gene: GTF3C1 general transcription factor IIIC, polypeptide 1, alpha 220kDa". Hsieh YJ, Kundu TK, Wang Z, Kovelman R, ... Meissner W, Thomae R, Seifart KH (2002). "The activity of transcription factor IIIC1 is impaired during differentiation of F9 ...
West AG, Shore P, Sharrocks AD (May 1997). "DNA binding by MADS-box transcription factors: a molecular mechanism for ... The MADS box encodes the DNA-binding MADS domain. The MADS domain binds to DNA sequences of high similarity to the motif CC[A/T ... 6GG termed the CArG-box. MADS-domain proteins are generally transcription factors. The length of the MADS-box reported by ... The MADS box protein structure is characterized by four domains. At the N terminal end is the highly conserved MADS DNA binding ...
These proteins are known as CCAAT box binding proteins/CCAAT box binding factors. A CCAAT box is a feature frequently found ... This box along with the GC box is known for binding general transcription factors. Both of these consensus sequences belong to ... The CAAT box signals the binding site for the RNA transcription factor, and is typically accompanied by a conserved consensus ... These core binding factors, or nuclear factors (NF-Y), are composed of three subunits - NF-YA, NF-YB, and NF-YC. Whereas in ...
"Identification of E-box factor TFE3 as a functional partner for the E2F3 transcription factor". Mol. Cell. Biol. 23 (11): 3707- ... TFE3, a member of the helix-loop-helix family of transcription factors, binds to the mu-E3 motif of the immunoglobulin heavy- ... Henthorn PS, Stewart CC, Kadesch T, Puck JM (Feb 1992). "The gene encoding human TFE3, a transcription factor that binds the ... "Entrez Gene: TFE3 transcription factor binding to IGHM enhancer 3". Giangrande PH, Hallstrom TC, Tunyaplin C, Calame K, Nevins ...
TATA-box binding protein associated factor 7 like is a protein that in humans is encoded by the TAF7L gene. This gene is ... "Entrez Gene: TATA-box binding protein associated factor 7 like". Retrieved 2018-03-03. Stouffs K, Willems A, Lissens W, ... similar to a mouse gene that encodes a TATA box binding protein-associated factor, and shows testis-specific expression. The ... encoded protein could be a spermatogenesis-specific component of the DNA-binding general transcription factor complex TFIID. ...
"Entrez Gene: NFX1 nuclear transcription factor, X-box binding 1". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method ... The protein encoded by this gene is a transcriptional repressor capable of binding to the conserved X box motif of HLA-DRA and ... II gene expression is controlled primarily at the transcriptional level by transcription factors that bind to the X and Y boxes ... "A novel cysteine-rich sequence-specific DNA-binding protein interacts with the conserved X-box motif of the human major ...
... a GC box-binding factor". J. Biochem. 121 (2): 389-96. doi:10.1093/oxfordjournals.jbchem.a021600. PMID 9089417. Cujec TP, Cho H ... 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding". J. Biol. Chem. 271 (20): 11703-9. doi:10.1074/jbc. ... "Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II". ... "HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors". Genes Dev. 6 (4): 655-66. ...
HES4, is a transcription factor found in humans. The protein binds DNA on N-box motifs. To date, the clinical significance of ... LRRIQ1 contains an IQ calmodulin-binding motif found in one isoform. The isoform contains three copies and serves as a binding ...
The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site. Factor Xa ... Factor X is activated, by hydrolysis, into factor Xa by both factor IX (with its cofactor, factor VIII in a complex known as ... The result is a Factor VIIa/TF complex, which catalyzes the activation of Factor X and Factor IX. Factor Xa formed on the ... Factor Xa plays a key role in all three of these stages. In stage 1, Factor VII binds to the transmembrane protein TF on the ...
A potential role for CArG-box binding factor-A in kappa transcription". J. Biol. Chem. 273 (30): 18881-90. doi:10.1074/jbc. ... "The B subunit of the CAAT-binding factor NFY binds the central segment of the Co-activator p300". J. Biol. Chem. 274 (12): 7623 ... Mantovani R (1999). "The molecular biology of the CCAAT-binding factor NF-Y". Gene. 239 (1): 15-27. doi:10.1016/S0378-1119(99) ... forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions in a ...
... is a nuclear protein that binds to DNA and acts as an architectural chromatin-binding factor. It can also be released ... High mobility group box 1 protein, also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a protein that in ... After binding, HMGB1 bends DNA, which facilitates the binding of other proteins. HMGB1 supports transcription of many genes in ... TLR4 binding by HMGB1 or LPS (lipopolysaccharide) sustains ADP-ribosylation of HMGB1 by PARP1 thereby serving as an ...
... and SPI1 bind to a purine-rich sequence, the PU box (5-prime-GAGGAA-3-prime).[supplied by OMIM] SPIB has been shown to ... "Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with ... Transcription factor Spi-B is a protein that in humans is encoded by the SPIB gene. SPI1 (MIM 165170) and SPIB are members of a ... Schotte R, Nagasawa M, Weijer K, Spits H, Blom B (December 2004). "The ETS transcription factor Spi-B is required for human ...
... also known as Y-box transcription factor or nuclease-sensitive element-binding protein 1 is a protein ... 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with ... the Y-box DNA/RNA-binding factor, YB-1, and the multivalent zinc finger factor, CTCF". J. Biol. Chem. 275 (38): 29915-21. doi: ... "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating ...
It activates transcription by binding to the E box (5'-CANNTG-3'). Dimerization with other BHLH proteins is required for ... This gene is a member of the basic helix-loop-helix (BHLH) family of transcription factors. ... "Transcription factor ASCL2 is required for development of the glycogen trophoblast cell lineage". PLOS Genetics. 14 (8): ... transcription factor family. ASCL2 is particularly important during implantation of the developing embryo, specifically in ...
E-box) sequences. In normal development, E proteins form dimers with other bHLH transcription factors, allowing transcription ... The first helix-loop-helix proteins identified were named E-proteins because they bind to Ephrussi-box ( ... ID proteins can bind E-proteins, preventing them from binding bHLH proteins and halting transcription, a case often seen in ... transcription factors to inhibit DNA binding of bHLH proteins. ID proteins also contain the HLH-dimerization domain but lack ...
Y-box-binding protein 2 is a protein that in humans is encoded by the YBX2 gene. RNA polymerase II Transcription (biology) ... 2009). "Sequence alterations in the YBX2 gene are associated with male factor infertility". Fertil. Steril. 91 (4): 1090-5. doi ... Tekur S, Pawlak A, Guellaen G, Hecht NB (Jul 1999). "Contrin, the human homologue of a germ-cell Y-box-binding protein: cloning ... 2006). "Expression of Y-box-binding protein dbpC/contrin, a potentially new cancer/testis antigen". Br. J. Cancer. 94 (5): 710- ...
"TAF15 TATA-box binding protein associated factor 15 [Homo sapiens (Human)] - Gene - NCBI". Rubin, Brian P.; Lazar, Alexander J. ... encoding an RNA-binding protein which is a component of transcription factor II D, TCF12 (15q21) encoding a transcription ... As often can be seen in chimeric transcripts including EWSR1, the transactivation domain of EWSR1 is fused to the DNA-binding ... In EMC the DNA-binding domain is constant and the transactivation domains of several genes are involved. These genes include ...
"DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in ... "FOXO4 forkhead box O4 [ Homo sapiens (human) ]". Weigel D, Jäckle H (Nov 1990). "The fork head domain: a novel DNA binding ... FOXO transcription factors have been shown to be the down downstream effector molecules of insulin-like growth factor (IGF) ... Tang TT, Lasky LA (2003). "The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 ...
... family of transcription factors. The protein activates transcription by binding to the E box (5'-CANNTG-3'). Dimerization with ... Long RM, Gu W, Meng X, Gonsalvez G, Singer RH, Chartrand P (April 2001). "An exclusively nuclear RNA-binding protein affects ... Delta can diffuse to neighboring cells and bind to the Notch receptor, a large transmembrane protein which upon activation ... First, it prevents the expression of factors required for differentiation of the cell into a neuroblast. Secondly, it inhibits ...
Molkentin JD, Li L, Olson EN (Jul 1996). "Phosphorylation of the MADS-Box transcription factor MEF2C enhances its DNA binding ... Myocyte-specific enhancer factor 2C also known as MADS box transcription enhancer factor 2, polypeptide C is a protein that in ... "Activated notch inhibits myogenic activity of the MADS-Box transcription factor myocyte enhancer factor 2C". Molecular and ... "Assignment of human myocyte-specific enhancer binding factor 2C (hMEF2C) to human chromosome 5q14 and evidence that MEF2C is ...
In molecular biology, TAFII28 refers to the TATA box binding protein associated factor. Together with the TATA-binding protein ... "Entrez Gene: TAF11 TAF11 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 28kDa". Birck C, Poch O, Romier C ... TAF11 has been shown to interact with: GTF2F1, POLR2A and TAF13, TAF15, TATA binding protein, and Transcription Factor II B. ... The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position ...
This gene belongs to subfamily P of the forkhead box (FOX) transcription factor family. Forkhead box transcription factors play ... Forkhead box P1 protein contains both DNA-binding- and protein-protein binding-domains. This gene may act as a tumor suppressor ... Foxp1 is a transcription factor; specifically it is a transcriptional repressor. Fox genes are part of a forkhead DNA-binding ... Li C, Tucker PW (1994). "DNA-binding properties and secondary structural model of the hepatocyte nuclear factor 3/fork head ...
The TATA box is the binding site of the TATA-binding protein (TBP) and other transcription factors in some eukaryotic genes. ... binds to the TATA box at its TATA-binding protein (TBP) subunit. TBP binds to the minor groove of the TATA box via a region of ... Gastric cancer is correlated with TATA box polymorphism. The TATA box has a binding site for the transcription factor of the ... TFIID first binds to the TATA box, facilitated by TFIIA binding to the upstream part of the TFIID complex. TFIIB then binds to ...
Region 2.4 recognizes and binds to the promoter −10 element (called the "Pribnow box"). Region 4.2 recognizes and binds to the ... Therefore, the sigma factor cycles between a strongly bound state during initiation and a weakly bound state during elongation ... Different sigma factors are utilized under different environmental conditions. These specialized sigma factors bind the ... A sigma factorfactor or specificity factor) is a protein needed for initiation of transcription in bacteria. It is a ...
TATA box binding protein (TBP)-associated factor, RNA polymerase I, D, 41kDa is a protein that in humans is encoded by the ... "Entrez Gene: TATA box binding protein (TBP)-associated factor, RNA polymerase I, D, 41kDa". Wang L, Bhattacharyya N, Chelsea DM ... Gorski JJ, Pathak S, Panov K, Kasciukovic T, Panova T, Russell J, Zomerdijk JC (March 2007). "A novel TBP-associated factor of ...
TATA box-binding protein-associated factor RNA polymerase I subunit B is an enzyme that in humans is encoded by the TAF1B gene ... "Entrez Gene: TAF1B TATA box binding protein (TBP)-associated factor, RNA polymerase I, B, 63kDa". Miller G, Panov KI, Friedrich ... and three TBP-associated factors (TAFs) specific for RNA polymerase I. This complex, known as SL1, binds to the core promoter ... Grandori C, Gomez-Roman N, Felton-Edkins ZA, Ngouenet C, Galloway DA, Eisenman RN, White RJ (2005). "c-Myc binds to human ...
TATA box-binding protein-associated factor RNA polymerase I subunit A is an enzyme that in humans is encoded by the TAF1A gene ... "Entrez Gene: TAF1A TATA box binding protein (TBP)-associated factor, RNA polymerase I, A, 48kDa". Seo SB, McNamara P, Heo S, ... and three TBP-associated factors (TAFs) specific for RNA polymerase I. This complex, known as selective factor 1 (SL1), binds ... Grandori C, Gomez-Roman N, Felton-Edkins ZA, Ngouenet C, Galloway DA, Eisenman RN, White RJ (2005). "c-Myc binds to human ...
An example p-box is shown in the figure at right for an uncertain number x consisting of a left (upper) bound and a right ( ... Augustsson, A., M. Filipsson, T. Öberg, B. Bergbäck (2011). Climate change-an uncertainty factor in risk analysis of ... the result is called a distributional p-box, or sometimes a parametric p-box. Such a p-box is usually easy to obtain by ... Its p-box is just a step function from 0 to 1 at the value c; mathematically this is {H(c), H(c), c, 0, H(c)}. P-boxes and ...
Augustsson, A., M. Filipsson, T. Öberg, B. Bergbäck (2011). Climate change-an uncertainty factor in risk analysis of ... Enszer, Joshua Alan, (2010). Verified Probability Bound Analysis for Dynamic Nonlinear Systems. Dissertation, University of ... P-boxes and probability bounds analysis have been used in many applications spanning many disciplines in engineering and ... Crespo, Luis G.; Kenny, Sean P.; Giesy, Daniel P. (2013). "Reliability analysis of polynomial systems subject to p-box ...
GCC box DNA-binding protein interacts with an ocs element binding protein". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5961-6. ... Riechmann JL, Meyerowitz EM (June 1998). "The AP2/EREBP family of plant transcription factors". Biol. Chem. 379 (6): 633-46. ... "A novel mode of DNA recognition by a beta-sheet revealed by the solution structure of the GCC-box binding domain in complex ... ethylene-responsive+element+binding+protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH) v t e ( ...
Protein target information for TATA-box binding protein associated factor 4 (Norway rat). Find diseases associated with this ...
Purification and characterization of a protein binding to the SP6 κ promoter : A potential role for CArG-box binding factor-A ... Purification and characterization of a protein binding to the SP6 κ promoter : A potential role for CArG-box binding factor-A ... box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different ... box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different ...
Brantjes H, Roose J, van De Wetering M, Clevers H (April 2001). "All Tcf HMG box transcription factors interact with Groucho- ... Its a member of T cell factor/lymphoid enhancer factor (TCF/LEF) family. Lymphoid enhancer-binding factor-1 (LEF1) is a 48-kD ... with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor ... with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor ...
Learn about Regulatory Factor X1 at online-medical-dictionary.org ... Regulatory Factor-X. Transcription Factor, RFX1. X Box Binding ... RF X Binding Protein. RF-X Binding Protein. RFX Regulatory Factor. RFX1 Protein. RFX1 Transcription Factor. Regulatory Factor X ... A regulatory factor X transcription factor that is required for the expression of MHC CLASS II GENES. It also binds to inverted ... Regulatory Factor X1. Synonyms. MHC Class II Regulatory Factor RFX. ...
Structure of the DNA-bound T-box domain of human TBX1, a transcription factor associated with the DiGeorge syndrome ... Structure of the DNA-bound T-box domain of human TBX1, a transcription factor associated with the DiGeorge syndrome ...
Human Estrogen Receptor Alpha Ligand-Binding Domain In Complex With OBCP-2M and A Glucocorticoid Receptor Interacting Protein 1 ... Receptor Alpha Ligand-Binding Domain In Complex With OBCP-2M and A Glucocorticoid Receptor Interacting Protein 1 NR Box II ... Classification: HORMONE/GROWTH FACTOR RECEPTOR. *Organism(s): Homo sapiens. *Expression System: Escherichia coli BL21(DE3) ... These agonists are 10-50-fold selective for ERbeta in competitive binding assays and up to 60-fold selective in transactivation ...
HMG-box, class I member of the HMG-box superfamily of DNA-binding proteins. These proteins contain a single HMG box, and bind ... SOX-TCF_HMG-box; class I member of the HMG-box superfamily of DNA-binding proteins. These proteins contain a single HMG box, ... SOX-TCF_HMG-box; class I member of the HMG-box superfamily of DNA-binding proteins. These proteins contain a single HMG box, ... SOX-TCF_HMG-box; class I member of the HMG-box superfamily of DNA-binding proteins. These proteins contain a single HMG box, ...
crystal structure of the rat vitamin D receptor ligand binding domain complexed with 2MD and a synthetic peptide containing the ... structure of the rat vitamin D receptor ligand binding domain complexed with 2MD and a synthetic peptide containing the NR2 box ... Classification: hormone/growth factor receptor. *Organism(s): Rattus norvegicus, Homo sapiens. *Expression System: Escherichia ... Binding of the 2-carbon-modified analogues does not change the positions of the amino acids in the ligand binding site and has ...
Regulatory Factor X Transcription Factors * Transcription Factors * X-Box Binding Protein 1 ...
TFIIIC box B-binding subunit. general transcription factor IIIC, polypeptide 1 (alpha subunit). general transcription factor ... Human transcription factor IIIC box B binding subunit. LEtoile ND, et al. Proc Natl Acad Sci U S A, 1994 Mar 1. PMID 8127861, ... B-block_TFIIIC; B-block binding subunit of TFIIIC. * NM_001520.4 → NP_001511.2 general transcription factor 3C polypeptide 1 ... GTF3C1 general transcription factor IIIC subunit 1 [Homo sapiens] GTF3C1 general transcription factor IIIC subunit 1 [Homo ...
A heteromeric transcription factor complex that binds to the CCAAT-box upstream of promoters; functions as both an activator ... Gene Ontology Term: CCAAT-binding factor complex. GO ID. GO:0016602 Aspect. Cellular Component. Description. ... CBF complex, NF-Y transcription factor complex, nuclear transcription factor Y complex View GO Annotations in other species in ... box at the top of the table. ... box at the top of the table. ...
We report here analysis of Tbx20 expression during murine cardiac development and assessment of DNA-binding and transcriptional ... Tbx20 is a member of the T-box transcription factor family expressed in the forming hearts of vertebrate and invertebrate ... Cardiac T-box factor Tbx20 directly interacts with Nkx2-5, GATA4, and GATA5 in regulation of gene expression in the developing ... Tbx20 is a member of the T-box transcription factor family expressed in the forming hearts of vertebrate and invertebrate ...
Transcription initiation factor IIA subunit 2: O. TATA-box-binding protein: P. General transcription factor IIE subunit 1: Q. ... General transcription factor IIF subunit 1: S. General transcription factor IIF subunit 2: T. SMTL:PDB. SMTL Chain Id:. PDB ... Transcription initiation factor IIB: M. Transcription initiation factor IIA subunit 1: N. ... Transcription initiation factor IIE subunit beta: R. ...
rbcS box III; 5 upstream region (-114) of pea rbcS gene; binding with trans factor GT-1; one of GT-1 boxes. ... rbcS G-box; 5upstream region (-211) of pea rbcS gene; binding with trans factor GBF (CG-1); Light-responsiveness. ... Box II of rice glutelin Gt2 gene family; nuclear factor binding site. ... Arabidopsis ethylene-responsive element binding factors act as transcriptional activators or repressors of GCC box-mediated ...
MADS domain transcription factors bind with a consensus sequence called the CArG box; The CArG boxes in the promoter of the ... Binding site of AP3/PI heterodimer; Binding site for a positively acting factors; ... Binding site page : Motif_111. Identifier. Motif_111. Name. CArG1 motif in AP3. Description. CArG1 found in the Arabidopsis ... APETALA3 (AP3) gene promoter; Binding site of AP3/PI heterodimer; ...
Segment boxes with dots indicate unknown genome sequences; TNFr, tumor necrosis factor receptor; U(fr), unknown fragment; ... epidermal growth factor; ChBP, chemokine binding protein; NMDAr, N-methyl D. -aspartate receptor-like protein. ... Gray boxes represent DNA sequence identity in the 2 genomes; black represents differences. The 2 large black boxes illustrate ... VirFHR, virulence factor host range; AnHR, ankyrin host range; IL18BP, interleukin 18 binding protein; UL, ubiquitin ligase; ...
Structure of the DNA-bound T-box domain of human TBX1, a transcription factor associated with the DiGeorge syndrome ... Structure of the DNA-bound T-box domain of human TBX1, a transcription factor associated with the DiGeorge syndrome ...
... resembles C3b and can bind to factor B (FB). FB is activated by factor D forming the alternative pathway C3 convertase. The ... Orange boxes highlight regulatory complement proteins. MBL: Mannose-binding lectin; MAC: Membrane attack complex; DAF: Decay ... C4b becomes membrane-bound and binds to pro-enzyme C2, which is then cleaved to C2a and C2b fragments by C1s. C2a remains bound ... C5b binds to C6 and C7, forming C5b67, which associates with an adjacent membrane. C5b67 then binds to C8 and multiple C9 ...
VEGF Vascular endothelial growth factor. XIAP X-linked inhibitor of apoptosis. ZEB1 or 2 Zinc finger E-box binding homeobox 1or ... Environmental factors and genetic factors are involved in the occurrence of this complication. Heredity is a major cause of ... Various factors are involved in the initiation and development of this process, perhaps the most important of which is VEGF ( ... Factors or compounds that can inhibit angiogenesis or disrupt the process in any way, may be good candidates for the treatment ...
The transcription factor TATA-box binding protein (TBP) modulates gene expression in nuclei. This process requires the ... in complex with TATA box binding protein and reveals a non-canonical function beyond nuclear transport that modulates TBP- ... Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding ... Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding ...
... insulin growth factor binding protein-1; HAND2, heart and neural crest derivative expressed 2; FOXO1, forkhead box 1; HOXA10, ... forkhead box 1 [FOXO1 (12, 60)]; homeobox A10 [HOXA10 (61)]; homeobox A11 [HOXA11 (62)]; SRY-Box transcription factor 4 [SOX4 ( ... Decidualization and insulin-like growth factor (IGF) binding protein: implications for its role in stromal cell differentiation ... SRY-Box transcription factor 4; SST, somatostatin; SCARA5, scavenger receptor class A member 5; DCN; decorin; IL15, interleukin ...
Growth differentiation factor 15. 5.90. 958.30. ENSG00000122728. TAF1L. TAF1-like RNA polymerase II, TATA box binding protein ( ... Latent transforming growth factor beta binding protein 1. 6.14. 129.49. ENSG00000048052. HDAC9. Histone deacetylase 9. 6.09. ... Ling, L.; Goeddel, D.V. MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule ... Complement factor H-related 5. −2.72. 0.37. 48 h. ENSG00000156475. PPP2R2B. Protein phosphatase 2, regulatory subunit B (PR 52) ...
I-box binding factor [Solanum lycopersicum]. arabidopsis. blastx. At5G04760.1. 218. 4e-57. 63.58. 507 bp (57.6%). 3. ... myb family transcription factor , chr5:1373753-1374530 REVERSE. swissprot. blastx. No significant hits ( or none blast was used ...
2007) Initiation of zebrafish haematopoiesis by the TATA-box-binding protein-related factor Trf3. Nature 450:1082-1085. ... The cells were then resuspended in 250 μl of binding buffer (10 mm HEPES, 140 mm NaCl, 2.5 mm CaCl2, pH 7.4) and incubated with ... 2004) BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha. J Exp Med 199:113- ... Lipocalin 2 (lcn2) is a member of the lipocalin family that binds to small hydrophobic molecules. We propose that lcn2 is an ...
RNA binding protein LARK might modulate stabilities of mRNAs coding some clock-output proteins. SLIMB is a F-box protein and ... Both groups of LNvs express the pigment-dispersing factor (pdf) gene, which is often used to reveal the projection pattern of ... This physical interaction prevents E-box-binding of CLK:CYC but does not disrupt the association between CLK and CYC (Lee et al ... Furthermore, the mCLK:BMAL1 heterodimer was shown to bind to the specific DNA element E-box having a nucleotide sequence CACGTG ...
Selecting the interface was another big factor. When choosing a standard router, users are bound by whatever interfaces that ... For example, an SD-WAN provider might provide you with a box that is licensed for 200-Mbps throughput. You will pay for the box ... There were other factors, too. From an engineering perspective, Intel offered chipsets with low power consumption, which helped ... Performance varies by use, configuration and other factors. // See our complete legal Notices and Disclaimers. // Intel is ...
In particular, mutations in DNA binding sites recognized by transcription factors can alter regulator binding affinities and, ... Here we present analysis of transcription factor binding motifs co-localized with non-coding variants. To avoid statistical ... Cancer somatic mutations in binding sites of selected transcription factors have been found under positive selection. However, ... Further analysis of transcription factors with conserved binding motifs can reveal cell regulatory pathways crucial for the ...
TATA-box binding protein associated factor 9b. Gene Type: protein-coding Organism: Homo sapiens Chromosome: X NCBI GeneID: ...
T-box transcription factor 21; TGF-β: transforming growth factor-β; TGFBI: transforming growth factor-beta-inducible gene h3; ... GATA binding protein 3 is a very important transcription factor in regulating the differentiation of T helper cells and the ... Aberrant DNA methylation of GATA binding protein 3 (GATA3), interleukin-4 (IL-4), and transforming growth factor-β (TGF-β) ... forkhead box protein 3; GATA3: GATA binding protein 3; H.pylori: Helicobacter pylori; IFN-γ: interferon-γ; IL: interleukin; ...
Name: TATA-box binding protein associated factor, RNA polymerase I, B. Synonyms: p63, A230108M10Rik, mTAFI68, 4930408G01Rik ...
  • A protein interacting with an A-T-rich region that is a positive control element within the SP6 κ promoter was purified and identified as CArG-box binding factor-A. The purified protein was shown to interact specifically with the coding strand of single-stranded DNA and, with lower affinity, with double-stranded DNA. (lu.se)
  • A mutation that inhibited binding of the protein to the A-T-rich region also aborted the transcriptional stimulatory effect of the region. (lu.se)
  • Two Ets proteins, PU.1 and elf-1, that have previously been shown to bind to an adjacent DNA element were shown to physically interact with CArG- box binding factor.A. An antiserum raised against the protein recognized two different forms indicating either that different splice-forms of. (lu.se)
  • Lymphoid enhancer-binding factor 1 (LEF1) is a protein that in humans is encoded by the LEF1 gene. (wikipedia.org)
  • Lymphoid enhancer-binding factor-1 (LEF1) is a 48-kD nuclear protein that is expressed in pre-B and T cells. (wikipedia.org)
  • To provide insight into the molecular mechanisms of their activity and selectivity, we determined the crystal structures of the ERalpha ligand-binding domain (LBD) and a peptide from the glucocorticoid receptor-interacting protein 1 (GRIP1) coactivator complexed with the ligands OBCP-3M, OBCP-2M, and OBCP-1M. (rcsb.org)
  • The transcription factor TATA-box binding protein (TBP) modulates gene expression in nuclei. (sinica.edu.tw)
  • The team led by Dr. Kuo-Chiang Hsia (Institute of Molecular Biology, Academia Sinica) and Dr. Wei-Yi Chen (Institute of Biochemistry and Molecular Biology, College of Life Sciences, National Yang Ming Chiao Tung University) presents a cryo-EM structure of Kap114p, one of the Kap-βs, in complex with TATA box binding protein and reveals a non-canonical function beyond nuclear transport that modulates TBP-dependent transcription. (sinica.edu.tw)
  • High-mobility group box 1 protein (HMGB1) has been reported to be a potent proangiogenic factor induced by inflammatory stress. (molvis.org)
  • The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. (antikoerper-online.de)
  • TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. (antikoerper-online.de)
  • This lack of transcription could be due to a mutation in the RBCS3A promoter creating the so-called F-box, a protein binding site located between the activating cis elements, the I-box and G-box. (wikiversity.org)
  • 1991), but to date no I-box binding protein has been cloned from plants. (wikiversity.org)
  • LeMYBI is the first isolated I-box binding protein and is a member of a novel class of myb-like proteins which to date is found exclusively in plants. (wikiversity.org)
  • Chronic ER stress promotes apoptosis, at least in part through the UPR-induced transcription factor C/EBP homologous protein (CHOP). (jci.org)
  • These findings suggest that CHOP is a fundamental factor that links protein misfolding in the ER to oxidative stress and apoptosis in β cells under conditions of increased insulin demand. (jci.org)
  • The sensors correspond to three branches of the UPR, namely protein kinase RNA-like endoplasmic reticulum kinase (PERK), activating transcription factor 6 (ATF6), and inositol-requiring enzyme 1 (IRE1) branches. (helsinki.fi)
  • It specifically targets X-box-binding protein 1 (XBP1) mRNA, from which a 26 nt intron is spliced. (helsinki.fi)
  • This allows a complete translation of spliced XBP1 mRNA into a functional protein that acts as a transcription factor. (helsinki.fi)
  • Initiation of transcription by RNA polymerase I requires the formation of a complex composed of the TATA-binding protein (TBP) and three TBP-associated factors (TAFs) specific for RNA polymerase I. This complex, known as SL1, binds to the core promoter of ribosomal RNA genes to position the polymerase properly and acts as a channel for regulatory signals. (avivasysbio.com)
  • The encoded protein contains two different binding sites that are known to bind DNA and function as a regulator of gene transcription. (biolegend.com)
  • STAT3 protein belongs to a group of intracellular transcription factors that mediate a variety of functions such as cellular differentiation, proliferation, and apoptosis. (biolegend.com)
  • The protein encoded by this gene is a member of the basic helix-loop-helix (bHLH) E-protein family that recognizes the consensus binding site (E-box) CANNTG. (novusbio.com)
  • Inactivation of TCF7L2 protein attained by removing the high-mobility group (HMG)-box DNA binding domain in mature adipocytes in vivo leads to whole-body glucose intolerance and hepatic insulin resistance. (medscape.com)
  • Consider an example with a single gene that is autoregula- tory, i.e. the transcription rate is enhanced when it is bound by its own protein product, X. There are then four possible states of the system. (lu.se)
  • In studying the parameter dependence of the binding strengths of the protein complexes on the three genes, we use the fact that the nature of the regulation on OCT4 and SOX2 is similar. (lu.se)
  • Human transcription factor IIIC box B binding subunit. (nih.gov)
  • In addition, this subunit interacts with the transcription factor CREB, which has a glutamine-rich activation domain, and binds to other proteins containing glutamine-rich regions. (antikoerper-online.de)
  • Aberrant binding to this subunit by proteins with expanded polyglutamine regions has been suggested as one of the pathogenetic mechanisms underlying a group of neurodegenerative disorders referred to as polyglutamine diseases. (antikoerper-online.de)
  • As in the case of the G box sequence, previous [ribulose-1,5-bisphosphate carboxylase small subunit] RBCS gene expression studies with transgenic plants have failed to demonstrate a requirement for these I box sequences, although mutation of what are likely to be functionally related sequences in CAB genes does affect expression (Gidoni et al. (wikiversity.org)
  • Epigenetic components (for example, Polycomb PRC1/2 and Trithorax group proteins) maintain the 'off' states of certain genes and the 'on' states of others, in a cell-type- and time-specific manner (the bottom panels show three genes, depicted schematically as chromatinized templates, in which transcription is triggered by specific transcription factors and silent or active states are maintained by PRC1/2 or Trithorax proteins, respectively). (nature.com)
  • The regulatory code is read by proteins called transcription factors that bind to short stretches of DNA called motifs. (tum.de)
  • When the population increases, the signal concentration elevates and at a threshold level the acyl-HSLs come in interaction with transcription factors like the LuxR proteins. (igem.org)
  • Transcription factors are proteins that regulate the transcription of genes, or the production of mRNA from DNA. (biolegend.com)
  • Intrinsically disordered proteins (IDPs) proteins lack stable folded structure under native conditions but can interact simultaneously with multiple partners and/or binding sites, thus facilitating rapid biological response to transient signals. (lu.se)
  • A regulatory factor X transcription factor that is required for the expression of MHC CLASS II GENES . (online-medical-dictionary.org)
  • Binding of TFIIIC to sine elements controls the relocation of activity-dependent neuronal genes to transcription factories. (nih.gov)
  • In particular, mutations in DNA binding sites recognized by transcription factors can alter regulator binding affinities and, consequently, expression of target genes. (biomedcentral.com)
  • The pluripotency of the initial cell and the establishment of cell types depend to a large extent on the coordinated deployment of hundreds of transcription factors that bind to specific DNA sequences to activate or repress the transcription of cell lineage genes 1 . (nature.com)
  • Experiments "show that site-specific mutations in either G or I, but not GT boxes, in the context of the full rbcS-IA promoter, drastically affect the rbcS-IA promoter-dependent expression of Adh and [ β -glucuronidas] GUS reporter genes. (wikiversity.org)
  • 1991). The first group consists of the RBCS1 , RBCS2 and RBCS3A genes, which contain a conserved pair of I-box (5'-GGATGA-GATAAGA-3') and G-box (5'-CACGTG-3') elements in an identical spatial arrangement (Manzara et al. (wikiversity.org)
  • In addition to environmental factors, phenotypes can also respond to genetic perturbations in a plastic or homeostatic manner, which characterizes the potential of an organism to express phenotypes when genes mutate. (nature.com)
  • That multimer is now able to activate the quorum sensing-regulated genes by binding the Lux box. (igem.org)
  • Hence, it is sufficient to study the parameter dependence of the binding at the NANOG gene and either of the OCT4 and SOX2 genes. (lu.se)
  • [ 4 ] The 6 genes involved in WS are PAX3 (encoding the paired box 3 transcription factor), MITF (microphthalmia-associated transcription factor), EDN3 (endothelin 3), EDNRB (endothelin receptor type B), SOX10 (encoding the Sry bOX10 transcription factor), and SNAI2 (snail homolog 2), with different frequencies. (medscape.com)
  • TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. (antikoerper-online.de)
  • It "appears that the RBCS2 promoter and, by extension, the RBCS1 and RBCS3A promoters, are activated by the co-ordinate binding of an I-box binding factor (IBF) and a G-box binding factor (GBF) in leaves, while the promoters are activated by a GBF alone in fruit. (wikiversity.org)
  • Their unique feature is their ability to bind DNA at sequences known as promoter or enhancer regions. (biolegend.com)
  • The sequence targeted by substitution P4 overlaps a sequence showing homology to the 'L' box (consensus 5'-AAATTAACCAA), which is conserved in RBCS upstream sequences of both tomato and tobacco (Giuliano et al. (wikiversity.org)
  • Predicted to enable DNA-binding transcription repressor activity, RNA polymerase II-specific and RNA polymerase II cis-regulatory region sequence-specific DNA binding activity. (nih.gov)
  • It binds to a functionally important site in the T-cell receptor-alpha (TCRA) enhancer and confers maximal enhancer activity. (wikipedia.org)
  • 2MbisP binds to the receptor despite the absence of the 25-hydroxyl group. (rcsb.org)
  • Lipocalin 2 (lcn2) is a member of the lipocalin family that binds to small hydrophobic molecules. (jneurosci.org)
  • It's a member of T cell factor/lymphoid enhancer factor (TCF/LEF) family. (wikipedia.org)
  • Once the transcription factor binds to an enhancer region, this can cause stimulation or repression of gene transcription. (biolegend.com)
  • RFX binds the X1 box of MHC-II promoters. (lu.se)
  • Among cardiac GATA factors, there was preferential synergy with GATA5, implicated in endocardial differentiation. (nih.gov)
  • Although "the P3, P6 substitutions alter the conserved 'GATAAG' I box motif, a 'GATA' motif is present in the introduced EcoRV site. (wikiversity.org)
  • RUNX1 belongs to the runt domain family of transcription factors and regulates target gene expression through forming a heterodimeric DNA-binding complex with CBFB. (biolegend.com)
  • This process requires the involvement of nuclear transport receptors, collectively termed karyopherin-ß (Kap-ß) in yeast, and various regulatory factors. (sinica.edu.tw)
  • They evaluate the changes in concentrations by comparing the number of bound receptors over the past 1s with the number during the past 3s. (igem.org)
  • We identified that vilazodone, an antidepressant, directly bound to TRIM21 to exert effective anti-metastatic action both in vitro and in vivo. (bvsalud.org)
  • It also binds to inverted repeats of HEPATITIS B VIRUS DNA and is required for viral gene expression. (online-medical-dictionary.org)
  • We report here analysis of Tbx20 expression during murine cardiac development and assessment of DNA-binding and transcriptional properties of Tbx20 isoforms. (nih.gov)
  • Tbx20 physically interacted with cardiac transcription factors Nkx2-5, GATA4, and GATA5, collaborating to synergistically activate cardiac gene expression. (nih.gov)
  • Although the majority of expression quantitative trait loci (eQTLs) for the gene expression traits in the two environments are shared and have similar effects, analysis of the environment-specific eQTLs reveals enrichment of binding sites for two transcription factors. (nature.com)
  • The capability of these cells to differentiate depends on the stem cell type, the regulation of gene expression by various transcription factors and interaction with the stem cell niche 1,4 . (biolegend.com)
  • RFX forms cooperative DNA binding complexes with x2bp and cbf/nf-y. (lu.se)
  • Binding strengths of the OCT4-SOX2 and OCT4-SOX2-NANOG complexes. (lu.se)
  • We therefore consider binding strengths a3 and a2 which determine how strongly OCT4-SOX2-NANOG and OCT4-SOX2 bind to OCT4, respectively, and e2 and e1, the binding strengths of the OCT4-SOX2-NANOG and OCT4-SOX2 complexes on the NANOG gene respectively (see Eq. (1) in the main text. (lu.se)
  • This is intuitively obvious, since the stronger that these complexes bind to OCT4, SOX2 and NANOG, the higher the transcription rate, and hence a smaller threshold of the environmental factor is required to turn the switch on. (lu.se)
  • Starting from the zygotic genome, stage- and cell-type-specific transcription factors initiate regulatory cascades that induce cell differentiation. (nature.com)
  • Part of transcription factor TFIIIC complex. (nih.gov)
  • function:Transcription factor required in complex with TAF3 for the differentiation of myoblasts into myocytes. (gbiosciences.com)
  • binds specifically to the I-box and activates transcription in yeast and plants. (wikiversity.org)
  • Further analysis of transcription factors with conserved binding motifs can reveal cell regulatory pathways crucial for the survivability of various human cancers. (biomedcentral.com)
  • Pax6 is a transcription factor present during embryonic development. (biolegend.com)
  • As a transcription factor, Pax6 acts at the molecular level in the signaling and formation of the central nervous system 11 . (biolegend.com)
  • Binding of the 2-carbon-modified analogues does not change the positions of the amino acids in the ligand binding site and has no effect on the interactions in the coactivator binding pocket. (rcsb.org)
  • The CD ring of the superpotent analogue, 2MD, is tilted within the binding site relative to the other ligands in this study and to (20S)-1alpha,25-dihydroxyvitamin D(3) [Tocchini-Valentini et al. (rcsb.org)
  • A water molecule is observed between His 301 and His 393 in this structure, and it preserves the orientation of the histidines in the binding site. (rcsb.org)
  • Isoforms with an intact T-box bound specifically to DNA sites resembling the consensus brachyury half site, although with less avidity compared with the related factor, Tbx5. (nih.gov)
  • associated Gene Ontology annotation of this binding site. (ugent.be)
  • Tbx20 is a member of the T-box transcription factor family expressed in the forming hearts of vertebrate and invertebrate embryos. (nih.gov)
  • We will present first molecular data showing how these boxes interact with critical transcription factors as well as with each other in a highly specific but also highly dynamic manner, and how these interactions can be interrupted. (lu.se)
  • Predicted to enable ATP binding activity and MAP kinase activity. (wormbase.org)
  • Cancer somatic mutations in binding sites of selected transcription factors have been found under positive selection. (biomedcentral.com)
  • For many transcription factors, including multiple members of FOX, HOX, and NR families, we show that human cancers accumulate fewer mutations than expected by chance that increase or decrease affinity of predicted binding sites. (biomedcentral.com)
  • the binding sites with a similar sequence. (ugent.be)
  • Our data demonstrate negative selection against binding sites alterations and suggest that such selection pressure protects cancer cells from rewiring of regulatory circuits. (biomedcentral.com)
  • Assessment of potential binding affinity changes induced by substitutions allows studying selection of sequence variants in binding sites in a way resembling usage of non-synonymous and synonymous substitutions in codons. (biomedcentral.com)
  • Among other objectives, these experiments attempted to identify factors that would either prolong or hasten the onset of respiratory arrest. (woodlibrarymuseum.org)
  • Together, the experiments done with cells transfected with CDNF, MANF or MANF mutants, suggested that the tested neurotrophic factors decreased IRE1 oligomerization and its activation. (helsinki.fi)
  • The key was to perform transcription factor-DNA binding experiments and computational modeling at the highest possible resolution, down to the level of individual DNA bases. (tum.de)
  • Change in genetic variation across environments is one of the many forms of genotype by environment interaction (G×E). G×E can be interpreted equivalently either as variable genetic architecture across environments or as variable environmental plasticity across genotypes, depending on what factor is chosen as the context. (nature.com)
  • The Role of MB0, MBI and MBII in Interaction and Dynamics of the Master Regulatory Transcription Factor c-Myc. (lu.se)
  • Located within the intrinsically disordered N-terminus part of c-Myc are the highly conserved so-called Myc boxes (MB0-IV), which are crucial for Myc function and interaction with other transcription factors. (lu.se)
  • Here we present analysis of transcription factor binding motifs co-localized with non-coding variants. (biomedcentral.com)
  • Transcription factor 7-like 2 (TCF7L2) variants have been associated with type 2 diabetes mellitus (T2DM) in multiple ethnic groups. (medscape.com)
  • This makes TCF7L2 variants the strongest known genetic risk factors for T2DM. (medscape.com)
  • Orthologous to human HBP1 (HMG-box transcription factor 1). (nih.gov)
  • Purification and characterization of two forms of human transcription factor IIIC. (nih.gov)
  • Is an ortholog of human FOXG1 (forkhead box G1). (wormbase.org)