Macromolecular complexes formed from the association of defined protein subunits.
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.
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.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
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.
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.
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.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
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.
Multiprotein complexes that mediate the activation of CASPASE-1. Dysregulation of inflammasomes has also been linked to a number of autoinflammatory and autoimmune disorders.
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.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
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.
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.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A retinoblastoma-binding protein that has an affinity for core HISTONES. It is found as a subunit of protein complexes that are in involved in the enzymatic modification of histones including the Mi2 and Sin3 histone deacetylase complexes and the polycomb repressive complex 2.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
Established cell cultures that have the potential to propagate indefinitely.
Methods for determining interaction between PROTEINS.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
Proteins found in any species of fungus.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Catalyzes the ATP-dependent PHOSPHORYLATION of GMP to generate GDP and ADP.
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.
An enzyme that catalyzes reversible reactions of a nucleoside triphosphate, e.g., ATP, with a nucleoside monophosphate, e.g., UMP, to form ADP and UDP. Many nucleoside monophosphates can act as acceptor while many ribo- and deoxyribonucleoside triphosphates can act as donor. EC
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.
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.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
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.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.
A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
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)
A large protein complex which acts as a signaling adaptor protein that allows communication between the various regulatory and functional components of GENETIC TRANSCRIPTION including DNA POLYMERASE II; GENERAL TRANSCRIPTION FACTORS; and TRANSCRIPTION FACTORS that are bound to upstream ENHANCER ELEMENTS. The mediator complex was originally studied in YEAST where at least 21 subunits were identified. Many of the yeast subunits are homologs to proteins in higher organisms that are found associated with specific nuclear receptors such as THYROID HORMONE RECEPTORS and VITAMIN D RECEPTORS.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A large class of structurally-related proteins that contain one or more LIM zinc finger domains. Many of the proteins in this class are involved in intracellular signaling processes and mediate their effects via LIM domain protein-protein interactions. The name LIM is derived from the first three proteins in which the motif was found: LIN-11, Isl1 and Mec-3.
A cellular transcriptional coactivator that was originally identified by its requirement for the stable assembly IMMEDIATE-EARLY PROTEINS of the HERPES SIMPLEX VIRUS. It is a nuclear protein that is a transcriptional coactivator for a number of transcription factors including VP16 PROTEIN; GA-BINDING PROTEIN; EARLY GROWTH RESPONSE PROTEIN 2; and E2F4 TRANSCRIPTION FACTOR. It also interacts with and stabilizes HERPES SIMPLEX VIRUS PROTEIN VMW65 and helps regulate GENETIC TRANSCRIPTION of IMMEDIATE-EARLY GENES in HERPES SIMPLEX VIRUS.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Proteins prepared by recombinant DNA technology.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
A multisubunit polycomb protein complex with affinity for CHROMATIN that contains methylated HISTONE H3. It contains an E3 ubiquitin ligase activity that is specific for HISTONE H2A and works in conjunction with POLYCOMB REPRESSIVE COMPLEX 2 to effect EPIGENETIC REPRESSION.
Trans-acting protein that combines with host factors to induce immediate early gene transcription in herpes simplex virus.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A broad category of nuclear proteins that are components of or participate in the formation of the NUCLEAR MATRIX.
A genus of ascomycetous yeast in the family Dipodascaceae, order SACCHAROMYCETALES.
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.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
A family of intracellular signaling adaptor proteins that contain caspase activation and recruitment domains. Proteins that contain this domain play a role in APOPTOSIS-related signal transduction by associating with other CARD domain-containing members and in activating INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.
Factors that associate with TATA-BOX BINDING PROTEIN. Many of them are components of TRANSCRIPTION FACTOR TFIID
Ribonucleic acid in protozoa having regulatory and catalytic roles as well as involvement in protein synthesis.
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 hemoflagellate subspecies of parasitic protozoa that causes nagana in domestic and game animals in Africa. It apparently does not infect humans. It is transmitted by bites of tsetse flies (Glossina).
A class of MOLECULAR CHAPERONES whose members act in the mechanism of SIGNAL TRANSDUCTION by STEROID RECEPTORS.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A species of fruit fly much used in genetics because of the large size of its chromosomes.
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 characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
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.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
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.
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.
Proteins found in any species of bacterium.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC
A ubiquitously expressed octamer transcription factor that regulates GENETIC TRANSCRIPTION of SMALL NUCLEAR RNA; IMMUNOGLOBULIN GENES; and HISTONE H2B genes.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules.
A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
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.
Large multiprotein complexes that bind the centromeres of the chromosomes to the microtubules of the mitotic spindle during metaphase in the cell cycle.
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.
Proteins found in any species of protozoan.
The process by which a DNA molecule is duplicated.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
A family of proteins that play a role in CHROMATIN REMODELING. They are best known for silencing HOX GENES and the regulation of EPIGENETIC PROCESSES.
Proteins that catalyze the unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. In addition DNA helicases are DNA-dependent ATPases that harness the free energy of ATP hydrolysis to translocate DNA strands.
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA.
A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins.
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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
The repeating structural units of chromatin, each consisting of approximately 200 base pairs of DNA wound around a protein core. This core is composed of the histones H2A, H2B, H3, and H4.
Proteins that are normally involved in holding cellular growth in check. Deficiencies or abnormalities in these proteins may lead to unregulated cell growth and tumor development.
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
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 type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.
Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.
Proteins obtained from ESCHERICHIA COLI.
A cell line derived from cultured tumor cells.
Proteins found in any species of insect.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
A type of FLUORESCENCE SPECTROSCOPY using two FLUORESCENT DYES with overlapping emission and absorption spectra, which is used to indicate proximity of labeled molecules. This technique is useful for studying interactions of molecules and PROTEIN FOLDING.
A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Chromatographic techniques in which the mobile phase is a liquid.
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
Cis-acting DNA sequences which can increase transcription of genes. Enhancers can usually function in either orientation and at various distances from a promoter.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
Complexes of RNA-binding proteins with ribonucleic acids (RNA).
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
Proteins obtained from the species Schizosaccharomyces pombe. 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.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
The sum of the weight of all the atoms in a molecule.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A serine threonine kinase that controls a wide range of growth-related cellular processes. The protein is referred to as the target of RAPAMYCIN due to the discovery that SIROLIMUS (commonly known as rapamycin) forms an inhibitory complex with TACROLIMUS BINDING PROTEIN 1A that blocks the action of its enzymatic activity.
Formation of an acetyl derivative. (Stedman, 25th ed)
Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
The clear constricted portion of the chromosome at which the chromatids are joined and by which the chromosome is attached to the spindle during cell division.
A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.
A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin. EC
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
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).
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.
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.
A technique for identifying specific DNA sequences that are bound, in vivo, to proteins of interest. It involves formaldehyde fixation of CHROMATIN to crosslink the DNA-BINDING PROTEINS to the DNA. After shearing the DNA into small fragments, specific DNA-protein complexes are isolated by immunoprecipitation with protein-specific ANTIBODIES. Then, the DNA isolated from the complex can be identified by PCR amplification and sequencing.
A plasma membrane exchange glycoprotein transporter that functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
Cell-cell junctions that seal adjacent epithelial cells together, preventing the passage of most dissolved molecules from one side of the epithelial sheet to the other. (Alberts et al., Molecular Biology of the Cell, 2nd ed, p22)
The rate dynamics in chemical or physical systems.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
The protein complement of an organism coded for by its genome.
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
The ultimate exclusion of nonsense sequences or intervening sequences (introns) before the final RNA transcript is sent to the cytoplasm.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
A large group of proteins that control APOPTOSIS. This family of proteins includes many ONCOGENE PROTEINS as well as a wide variety of classes of INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS such as CASPASES.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
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.
Detergent-insoluble CELL MEMBRANE components. They are enriched in SPHINGOLIPIDS and CHOLESTEROL and clustered with glycosyl-phosphatidylinositol (GPI)-anchored proteins.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The functional hereditary units of FUNGI.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
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.
Deoxyribonucleic acid that makes up the genetic material of fungi.
Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.

Self-regulated polymerization of the actin-related protein Arp1. (1/5719)

The actin-related protein Arp1 (or centractin, actin RPV) is the major subunit of dynactin, a key component of the cytoplasmic dynein motor machinery [1] [2] [3]. Of the ubiquitously expressed members of the Arp superfamily, Arp1 is most similar to conventional actin [4] [5] [6] and, on the basis of conserved sequence features, is predicted to bind ATP and possibly polymerize. In vivo, all cytosolic Arp1 sediments at 20S [7] suggesting that it assembles into oligomers, most likely dynactin - a multiprotein complex known to contain eight or nine Arp1 monomers in a 37 nm filament [8]. The uniform length of Arp1 polymers suggests a novel assembly mechanism that may be governed by a 'ruler' activity. In dynactin, the Arp1 filament is bounded by actin-capping protein at one end and a heterotetrameric protein complex containing the p62 subunit (D.M. Eckley, S.R. Gill, J.B.B., J.E. Heuser, T.A.S., unpublished observations) at the other [8]. In the present study, we analyzed the behavior of highly purified, native Arp1. Arp1 was found to polymerize rapidly into short filaments that were similar, but not identical, in length to those in dynactin. With time, these filaments appeared to anneal to form longer assemblies but never attained the length of conventional actin filaments.  (+info)

A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex. (2/5719)

Nuclear receptors play critical roles in the regulation of eukaryotic gene expression. We report the isolation and functional characterization of a novel transcriptional coactivator, termed steroid receptor RNA activator (SRA). SRA is selective for steroid hormone receptors and mediates transactivation via their amino-terminal activation function. We provide functional and mechanistic evidence that SRA acts as an RNA transcript; transfected SRA, unlike other steroid receptor coregulators, functions in the presence of cycloheximide, and SRA mutants containing multiple translational stop signals retain their ability to activate steroid receptor-dependent gene expression. Biochemical fractionation shows that SRA exists in distinct ribonucleoprotein complexes, one of which contains the nuclear receptor coactivator steroid receptor coactivator 1. We suggest that SRA may act to confer functional specificity upon multiprotein complexes recruited by liganded receptors during transcriptional activation.  (+info)

The N-terminal transactivation domain of ATF2 is a target for the co-operative activation of the c-jun promoter by p300 and 12S E1A. (3/5719)

The adenovirus E1A proteins activate the c-jun promoter through two Jun/ATF-binding sites, jun1 and jun2. P300, a transcriptional coactivator of several AP1 and ATF transcription factors has been postulated to play a role in this activation. Here, we present evidence that p300 can control c-jun transcription by acting as a cofactor for ATF2: (1) Over-expression of p300 was found to stimulate c-jun transcription both in the presence and absence of E1A. (2) Like E1A, p300 activates the c-jun promoter through the junl and jun2 elements and preferentially activates the N-terminal domain of ATF2. (3) Co-immunoprecipitation assays of crude cell extracts indicate that endogenous p300/CBP(-like) proteins and ATF2 proteins are present in a multiprotein complex that can bind specifically to the jun2 element. We further demonstrate that the Stress-Activated-Protein-Kinase (SAPK) target sites of ATF2, Thr69 and Thr71 are not required for the formation of the p300/CBP-ATF2 multiprotein complex. These data indicate that E1A does not inhibit all transcription activation functions of p300, and, in fact, cooperates with p300 in the activation of the ATF2 N-terminus.  (+info)

Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of the COP9 complex. (4/5719)

The COP9 complex is a regulator essential for repression of light-mediated development in Arabidopsis. Using partial amino acid sequence data generated from purified COP9 complexes, we cloned the Arabidopsis cDNA encoding the 27-kD subunit of the COP9 complex and showed that it is encoded by the previously identified FUSCA5 (FUS5) locus. fus5 mutants exhibit constitutive photomorphogenic phenotypes similar to those of cop9 and fus6. Point mutations in FUS5 that led to a loss of FUS5 protein were detected in four fus5 allelic strains. FUS5 contains the PCI/PINT and mitogen-activated protein kinase kinase activation loop motifs and is highly conserved with the mammalian COP9 complex subunit 7 and the Aspergillus nidulans AcoB proteins. FUS5 is present in both complex and monomeric forms. In the COP9 complex, FUS5 may interact directly with FUS6 and COP9. Mutations in FUS6 and COP9 result in a shift in the electrophoretic mobility of FUS5. This shift can be mimicked by in vitro phosphorylation of FUS5 by plant extracts. These findings further support the hypothesis that the COP9 complex is a central and common regulator that may interact with multiple signaling pathways.  (+info)

Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. (5/5719)

Recently we identified a novel human (h) multiprotein complex, called TATA-binding protein (TBP)-free TAFII-containing complex (TFTC), which is able to nucleate RNA polymerase II transcription and can mediate transcriptional activation. Here we demonstrate that TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. The recently described TRRAP cofactor for oncogenic transcription factor pathways was also characterized as a TFTC subunit. Furthermore, we identified four other previously uncharacterized subunits of TFTC: hADA3, hTAFII150, hSPT3, and hPAF65beta. Thus, the polypeptide composition of TFTC suggests that TFTC is recruited to chromatin templates by activators to acetylate histones and thus may potentiate initiation and activation of transcription.  (+info)

Maternal histone deacetylase is accumulated in the nuclei of Xenopus oocytes as protein complexes with potential enzyme activity. (6/5719)

Reversible acetylation of core histones plays an important regulatory role in transcription and replication of chromatin. The acetylation status of chromatin is determined by the equilibrium between activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). The Xenopus protein HDACm shows sequence homology to other putative histone deacetylases, but its mRNA is expressed only during early development. Both HDACm protein and acetylated non-chromosomal histones are accumulated in developing oocytes, indicating that the key components for histone deposition into new chromatin during blastula formation are in place by the end of oogenesis. Here we show that the 57 kDa HDACm protein undergoes steady accumulation in the nucleus, where it is organized in a multiprotein complex of approx. 300 kDa. A second, major component of the nuclear complex is the retinoblastoma-associated protein p48 (RbAp48/46), which may be used as an adaptor to contact acetylated histones in newly assembled chromatin. The nuclear complex has HDAC activity that is sensitive to trichostatin A, zinc ions and phosphatase treatment. The 57 kDa protein serves as a marker for total HDAC activity throughout oogenesis and early embryogenesis. The active HDACm complex and its acetylated histone substrates appear to be kept apart until after chromatin assembly has taken place. However, recombinant HDACm, injected into the cytoplasm of oocytes, not only is translocated to the nucleus, but also is free to interact with the endogenous chromatin.  (+info)

Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing. (7/5719)

Myb-related cdc5p is required for G(2)/M progression in the yeast Schizosaccharomyces pombe. We report here that all detectable cdc5p is stably associated with a multiprotein 40S complex. Immunoaffinity purification has allowed the identification of 10 cwf (complexed with cdc5p) proteins. Two (cwf6p and cwf10p) are members of the U5 snRNP; one (cwf9p) is a core snRNP protein. cwf8p is the apparent ortholog of the Saccharomyces cerevisiae splicing factor Prp19p. cwf1(+) is allelic to the prp5(+) gene defined by the S. pombe splicing mutant, prp5-1, and there is a strong negative genetic interaction between cdc5-120 and prp5-1. Five cwfs have not been recognized previously as important for either pre-mRNA splicing or cell cycle control. Further characterization of cwf1p, cwf2p, cwf3p, and cwf4p demonstrates that they are encoded by essential genes, cosediment with cdc5p at 40S, and coimmunoprecipitate with cdc5p. We further show that cdc5p associates with the U2, U5, and U6 snRNAs and that cells lacking cdc5(+) function are defective in pre-mRNA splicing. These data raise the possibility that the cdc5p complex is an intermediate in the assembly or disassembly of an active S. pombe spliceosome.  (+info)

Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. (8/5719)

Genetic screens for modifiers of activated Ras phenotypes have identified a novel protein, kinase suppressor of Ras (KSR), which shares significant sequence homology with Raf family protein kinases. Studies using Drosophila melanogaster and Caenorhabditis elegans predict that KSR positively regulates Ras signaling; however, the function of mammalian KSR is not well understood. We show here that two predicted kinase-dead mutants of KSR retain the ability to complement ksr-1 loss-of-function alleles in C. elegans, suggesting that KSR may have physiological, kinase-independent functions. Furthermore, we observe that murine KSR forms a multimolecular signaling complex in human embryonic kidney 293T cells composed of HSP90, HSP70, HSP68, p50(CDC37), MEK1, MEK2, 14-3-3, and several other, unidentified proteins. Treatment of cells with geldanamycin, an inhibitor of HSP90, decreases the half-life of KSR, suggesting that HSPs may serve to stabilize KSR. Both nematode and mammalian KSRs are capable of binding to MEKs, and three-point mutants of KSR, corresponding to C. elegans loss-of-function alleles, are specifically compromised in MEK binding. KSR did not alter MEK activity or activation. However, KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions. Together, these results suggest that KSR may act as a scaffolding protein for the Ras-mitogen-activated protein kinase pathway.  (+info)

CHROMOSOMES undergo dynamic behaviors during mitosis to enable the precise separation of the two replicated sister chromatids. It is vital that the replicated sister chromatids are separated successfully. There are two crucial prerequisites for accurate segregation: (1) cohesion between the replicated chromatids must be maintained until anaphase and (2) compaction of the chromosomes into a manageable form, condensation, must be completed prior to metaphase. These processes require two major protein complexes, the cohesin and condensin complexes. Each of these complexes is founded upon a heterodimer of structural maintenance of chromosomes (SMC) proteins, which are chromosome-associated ATPases (Hirano 1998, 2002). Also within each complex are two or three non-SMC subunits, which attribute specific functions to the SMC holocomplex. Despite a similar structural paradigm, the condensin and cohesin complexes are functionally distinct. Although each complex was originally identified for unique ...
Growth of an organ during development and during adaptation in the adult can be controlled by alterations either in the number or the size of cells. The two mechanisms are fundamentally different and require distinct regulation. Rapamycin is a cell growth inhibitor used to treat a number of clinical indications including graft rejection and cancer. The molecular target of rapamycin is a Ser/Thr kinase, called TOR in yeast or mTOR in mammals. The evolutionarily conserved TOR pathway controls key aspects of cellular growth and metabolism. Among these are protein synthesis, ribosome biogenesis, nutrient transport and processing, autophagy and mitochondrial function. mTOR assembles into two distinct multiprotein complexes, termed mTORC1 and mTORC2. mTORC1 consists of raptor (regulatory associated protein of mTOR), mLST8 (mammalian lethal with SEC13 protein 8) and mTOR, and is sensitive to rapamycin. mTORC2 consists of rictor (rapamycin insensitive companion of mTOR), mSIN1, mLST8 (mammalian stress ...
Transcriptional repression is a general mechanism for regulating transcriptional initiation in organisms ranging from yeast to humans. Accurate initiation of transcription from eukaryotic protein-encoding genes requires the assembly of a large multiprotein complex consisting of RNA polymerase II and general transcription factors such as TFIIA, TFIIB, and TFIID. DR1 is a repressor that interacts with the TATA-binding protein (TBP) of TFIID and prevents the formation of an active transcription complex by precluding the entry of TFIIA and/or TFIIB into the preinitiation complex. The protein encoded by this gene is a corepressor of transcription that interacts with DR1 to enhance DR1-mediated repression. The interaction between this corepressor and DR1 is required for corepressor function and appears to stabilize the TBP-DR1-DNA complex. [provided by RefSeq, Jul 2008 ...
We are witnessing tremendous improvements in our understanding of the organization of existence. towards large multiprotein complexes, in particular in eukaryotes, right now calls for a similarly concerted effort to develop and provide new technologies that are urgently required to create in quality and amount the plethora of multiprotein assemblies that form the complexome, and to regularly study their structure and function in the molecular level. Current attempts towards this objective are summarized and examined with this contribution. a two-step process that yields undamaged protein complexes composed of the tagged bait and any connected partners. This method is particularly useful for detecting stable complexes; more transient complexes are not observed, as they tend to dissociate during purification. Two major proteome-wide studies in using the Faucet method have exposed many previously unfamiliar protein relationships and pathway associations [8, 9]. In one study, Gavin genome which ...
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity).
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes ...
This gene encodes a component of the 26S proteasome. The 26S proteasome is a large multiprotein complex that catalyzes the degradation of ubiquitinated intracellular proteins. The encoded protein is a component of the 19S regulatory cap complex of the 26S proteasome and mediates substrate deubiquitination. A pseudogene of this gene is also located on the long arm of chromosome 2 ...
Protein target information for Condensin complex subunit 1 (zebrafish). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
View mouse Ncapg2 Chr12:116405355-116463532 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
TY - JOUR. T1 - Binding Specificity of Multiprotein Signaling Complexes Is Determined by Both Cooperative Interactions and Affinity Preferences. AU - Houtman, Jon C.D.. AU - Higashimoto, Yuichiro. AU - Dimasi, Nazzareno. AU - Cho, Sangwoo. AU - Yamaguchi, Hiroshi. AU - Bowden, Brent. AU - Regan, Carole. AU - Malchiodi, Emilio L.. AU - Mariuzza, Roy. AU - Schuck, Peter. AU - Appella, Ettore. AU - Samelson, Lawrence E.. PY - 2004/4/13. Y1 - 2004/4/13. N2 - The generation of multiprotein complexes at receptors and adapter proteins is crucial for the activation of intracellular signaling pathways. In this study, we used multiple biochemical and biophysical methods to examine the binding properties of several SH2 and SH3 domain-containing signaling proteins as they interact with the adapter protein linker for activation of T-cells (LAT) to form multiprotein complexes. We observed that the binding specificity of these proteins for various LAT tyrosines appears to be constrained both by the affinity of ...
proteopedia link. Many PDB files contain complexes in which a particular protein is interacting with a different protein in what are called multi-protein assemblies or multi-protein complexes. These interactions, if biologically relevant, can be immensely insightful in shedding light on cellular and extracellular processes. ...
The Target of Rapamycin (TOR) is a conserved serine/threonine (ser/thr) kinase that functions in two, distinct, multiprotein complexes called TORC1 and TORC2. Each complex regulates different aspects of eukaryote growth: TORC1 regulates cell volume and/or mass by influencing protein synthesis and tu …
The COP9 signalosome (CSN) is a conserved protein complex, typically composed of eight subunits (designated as CSN1 to CSN8) in higher eukaryotes such as ...
Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex (By similarity). The CSN complex is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of PSIAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. Not involved in CSNs deneddylation/derubylation activity (PubMed:15486099, PubMed:17307927). Essential for
Condensins are pentameric complexes that were initially described as being involved in the dynamics of chromosomes during mitosis. It has been recently established that two related complexes (Condensin I and Condensin II) contribute to this process. An increasing sum of studies, using different approaches in various organisms, leads to the paradigm that Condensins are required for the correct segregation of replicated chromosomes by cooperating somehow with Topoisomerase II in sister chromatid resolution. Depending on species and/or experimental studies, these complexes also contribute to some aspects of the assembly and compaction of mitotic chromosomes. Recent studies provided evidences that Condensins and related complexes also function in non-mitotic processes such as replication and transcription. Biochemical studies have highlighted mechanistic aspects of Condensin function and initiated a fine functional dissection of core and regulatory subunits. However, the exact contribution of each subunit
We used the tracking data to determine the velocity and processivity of wild-type condensin. A plot of the velocity distributions for data collected in the presence of saturated concentrations of ATP (4 mM; Fig. 1G) was well described by a log-normal distribution, revealing a mean apparent translocation velocity of 63 ± 36 base pairs (bp) s−1 (16 ± 9 nm s−1; means ± SD; n = 491) (Fig. 3E). Upon initial binding, condensin paused for a brief period (τpause = 13.3 ± 1.5 s; mean ± SD) before beginning to move along the DNA, which suggests the existence of a rate-limiting step before condensin becomes active for translocation (Fig. 2C and fig. S5). Each translocating condensin complex remained bound to the DNA for an average total time of 4.7 ± 0.2 min and traveled an average of 10.3 ± 0.4 kb (2.6 ± 0.1 μm; means ± SD) before dissociating (Fig. 3F and fig. S6A). These values provide merely a lower limit of the processivity of condensin, because a considerable fraction (42%) of the ...
WD40 domains are abundant in eukaryotes, and they are essential subunits of large multiprotein complexes, which serve as scaffolds. WD40 proteins participate in various cellular processes, such as histone modification, transcription regulation, and signal transduction. WD40 proteins are regarded as crucial regulators of plant development processes. However, the systematic identification and analysis of WD40 proteins have yet to be reported in wheat. In this study, a total of 743 WD40 proteins were identified in wheat, and they were grouped into 5 clusters and 11 subfamilies. Their gene structures, chromosomal locations, and evolutionary relationships were analyzed. Among them, 39 and 46 pairs of TaWD40s were distinguished as tandem duplication and segmental duplication genes. The 123 OsWD40s were identified to exhibit synteny with TaWD40s. TaWD40s showed the specific characteristics at the reproductive developmental stage, and numerous TaWD40s were involved in responses to stresses, including cold, heat
DELLA protein RGA; Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Positively regulates XERICO expression in seeds. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Compared to other DELLA proteins, it is the most sensitive to GA application. No effect of the BOI proteins on its stability. Its activity is probably regulated by other phytohormones such as auxin and ethylene, attenu [...] (587 aa ...
The mechanisms by which nuclear receptors transmit a hormone binding signal to core transcription machinery have been the focus of intensive research. These efforts have lead to the identification and characterization of several distinct multiprotein complexes which directly interact with agonist-bound nuclear receptors (9, 16, 28, 45, 46). The SRC-1 family of nuclear receptor coactivators appear to play a critical role in mediating the association of one of these complexes to nuclear receptors. This complex has been shown to contain potent HAT activities in p300-CBP and also the p300/CBP-associated factor PCAF. Additionally, these factors have been identified in complexes that contain intrinsic chromatin remodeling activity. These findings suggest that the SRC-1-containing complex may have as its primary purpose the chemical modification of the chromatin surrounding a target gene to which it is recruited. A second complex, identified on the basis of its ability to interact with activated ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Background Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating...
Losada, A., Yokochi, T., Hirano, T. (May 2005) Functional contribution of Pds5 to cohesin-mediated cohesion in human cells and Xenopus egg extracts. J Cell Sci, 118 (Pt 10). pp. 2133-41. ISSN 0021-9533 (Print) Ono, T., Losada, A., Hirano, M., Myers, M. P., Neuwald, A. F., Hirano, T. (October 2003) Differential contributions of condensin I and condensin II to mitotic chromosome architecture in vertebrate cells. Cell, 115 (1). pp. 109-121. ISSN 0092-8674 Losada, A., Hirano, M., Hirano, T. (December 2002) Cohesin release is required for sister chromatid resolution, but not for condensin-mediated compaction, at the onset of mitosis. Genes & Development, 16 (23). pp. 3004-3016. ISSN 0890-9369 MacCallum, D. E., Losada, A., Kobayashi, R., Hirano, T. (January 2002) ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-aurora B. Molecular Biology of the Cell, 13 (1). pp. 25-39. ISSN 1059-1524 Losada, A., Hirano, T. (October 2001) ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
This gene encodes a subunit of the condensin complex, which is responsible for the condensation and stabilization of chromosomes during mitosis and meiosis. Phosphorylation of the encoded protein activates the condensin complex. There are pseudogenes for this gene on chromosomes 8 and 15. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2012] ...
Mammalian cell growth is tightly linked to adequate supplies of growth factors and nutrients, including glucose and amino acids. The mechanistic target of rapamycin complex 1 (mTORC1) functions as a coincidence detector that supports anabolic metabolism when convergent growth factor- and nutrient-derived signals trigger mTORC1 kinase activation. Conversely, nutrient starvation suppresses mTORC1 activity and triggers a shift to catabolic pathways, such as autophagy, to support cell survival under austere conditions. An elaborate signaling apparatus has evolved to harmonize mTORC1 kinase activation and protein synthesis with supplies of leucine and other amino acids (1). Earlier findings implicated the leucyl-transfer RNA (tRNA) synthetase 1 (LARS1) as a proximate sensor of leucine availability (2). On page 205 of this issue, Yoon et al. (3) report that glucose modulates the functions of LARS1 in leucine sensing and disposition, thereby coordinating leucine-dependent mTORC1 activation and protein ...
The mechanistic target of rapamycin complex 1 (mTORC1) is a central regulator of cell growth and proliferation that is often aberrantly activated in cancer, as...
Background In addition to serving as building blocks for protein synthesis, amino acids also provide energy and precursors that are used by cells through catabolism. Mechanistic target of rapamycin complex 1 (mTORC1) is a central coordinator of cellular metabolism. However, little is known regar...
概要:哺乳动物雷帕霉素靶蛋白复合物1(mTORC1)能够感受一系列细胞内外的环境因素(如氨基酸),从而控制细胞生长和代谢.在过去的几十年里,众多蛋白被发现能够参与受氨基酸调控的mTORC1信号通路中.Rag GTPases能够将氨基酸的信号传递给mTORC1并招募mTORC1到溶酶体表面.近年来,参与mTORC1信号通路的蛋氨酸代谢物、亮氨酸以及精氨酸的感受体逐渐被发现.感受体的鉴定有助于理解细胞是如何通过调整内部氨基酸感应通路来满足自身需求.本文综述了氨基酸调控mTORC1信号通路的分子机制,并探讨了感受体如何将特定氨基酸信号精确传递给mTORC1信号通路 ...
DEPTOR [DEP-domain-containing and mTOR (mammalian target of rapamycin)-interacting protein] is a modulator of mTOR signalling that binds to mTORC (mTOR complex) 1 and mTORC2. However, to date, the precise functions of DEPTOR are not fully elucidated,
HCAP-G antibody (non-SMC condensin I complex, subunit G) for WB. Anti-HCAP-G pAb (GTX131128) is tested in Human samples. 100% Ab-Assurance.
Multiprotein complexes are an emerging focus in current biology, resulting in a demand for advanced heterologous expression systems
The inflammasome is a multi-protein complex which when activated regulates caspase-1 activation and IL-1β and IL-18 secretion. The NLRP3 (NACHT, LRR, and pyrin ...
Interaction between NBS1 and the mTOR/Rictor/SIN1 complex.A & B. Co-immunoprecipitation assays showed the interaction between NBS1 and mTOR in 293T cells ov
UNFCCC COP21大會期間,編輯室與特約記者、合作媒體ENS現場連線,並與譯者合作盤整談判重點做成即時報導,傳遞第一手消息,文章將同步與台達電子文教基金會低碳生活部落格、CNEX 紀實頻道共同刊登。此為「COP21連線」四項子專題之四。各項子專題請見 COP21翻譯米糕|COP21×社群觀點|COP21會前情勢|COP21大會連線
In a blind test of protein-docking algorithms, six groups used different methods to predict the structure of a protein complex. All six predicted structures were close enough to the experimental complex to be useful; nevertheless, several important details of the experimental complex were missed or …
Histones are modified at specific positions on their conserved amino‐terminal tails, and these modifications play central roles in gene regulation (Jenuwein and Allis, 2001; Turner, 2002). For example, acetylation at lysine 14 of histone H3 (H3K14Ac) or methylation of lysine 4 (H3K4Me) is associated with gene activation. In contrast, the lack of acetylation as well as the methylation of lysine 9 of histone H3 (H3K9Me) is correlated with gene repression (Jenuwein and Allis, 2001; Turner, 2002). These two types of modifications are performed by histone acetyltransferases (HATs) and histone methyltransferases (HMTases). These modifying enzymes are members of large multiprotein complexes with other subunits likely serving roles in targeting or regulation. The primary substrates for these enzymes are the amino‐terminal tails of the histone proteins. Modified tails function as binding platforms for transcriptional regulatory factors. For example, the histone H3 tail methylated at lysine 9 is ...
Chloroplasts originated from an endosymbiotic event in which a free-living cyanobacterium was engulfed by an ancestral eukaryotic host. During evolution the majority of the chloroplast genetic information was transferred to the host cell nucleus. As a consequence, proteins formerly encoded by the chloroplast genome are now translated in the cytosol and must be subsequently imported into the chloroplast. This process involves three steps: (i) cytosolic sorting procedures, (ii) binding to the designated receptor-equipped target organelle and (iii) the consecutive translocation process. During import, proteins have to overcome the two barriers of the chloroplast envelope, namely the outer envelope membrane (OEM) and the inner envelope membrane (IEM). In the majority of cases, this is facilitated by two distinct multiprotein complexes, located in the OEM and IEM, respectively, designated TOC and TIC. Plants are constantly exposed to fluctuating environmental conditions such as temperature and light ...
The mammalian target of rapamycin complex 1 (mTORC1) is mixed up in cellular transcription and translation processes. in control (P) bodies a niche site for mRNA degradation. Incubation of cells with rapamycin a known inhibitor of mTOR kinase activity improved the full total Edc4 proteins expression but at the same time reduced the Edc4 discussion with mTORC1. Furthermore rapamycin treatment led to a significant reduction in total serine phosphorylated Edc4 proteins signal and the full total 5′-capped mRNA. These results provide the 1st proof for the pivotal part of mTORC1 in Edc4 rules. Further in-depth research must get a full knowledge of molecular crosstalk between mTORC1 signaling and mRNA decapping pathway. and axis. Statistical relationship using Pearsons technique [22] for just two 3rd party tests demonstrated coefficients of 0.863 and 0.754 respectively which recommended a high level of co-occurrence of the raptor element of Edc4 and mTORC1. Likewise the Manders overlap coefficients ...
Two simple models can be envisaged: either cohesins are needed to activate condensin function or, alternatively, cohesins are required to ensure correct chromosome folding by condensins. These models can be distinguished by following the state of the mitotic chromosomes after a loss of cohesin activity. In the first scenario, the chromosomes remain in an interphase state, and thus would condense upon the readdition of cohesin and the subsequent activation of condensin. In contrast, the latter scenario predicts that misfolded chromosomes would result from the inappropriate action of condensin, and these would likely prove refractory to refolding. To test this, we asked whether chromosome condensation is reversible in the cohesin mutant mcd1-1. In contrast to both the brn1-9 and ycg1-2 condensin mutants, the condensation defect in the mcd1-1 strain was not reversible (Fig. 7 B). One trivial explanation is that no new functional Mcd1-1p protein is made after the shift to the permissive ...
The mechanistic (or mammalian) target of rapamycin complex 1 (mTORC1) controls cell growth, proliferation, and metabolism in response to diverse stimuli. Two major parallel pathways are implicated in mTORC1 regulation including a growth factor-responsive pathway mediated via TSC2/Rheb and an amino acid-responsive pathway mediated via the Rag GTPases. Here, we identify and characterize three highly conserved growth factor-responsive phosphorylation sites on RagC, a component of the Rag heterodimer, implicating cross talk between amino acid and growth factor-mediated regulation of mTORC1. We find that RagC phosphorylation is associated with destabilization of mTORC1 and is essential for both growth factor and amino acid-induced mTORC1 activation. Functionally, RagC phosphorylation suppresses starvation-induced autophagy, and genetic studies in reveal that RagC phosphorylation plays an essential role in regulation of cell growth. Finally, we identify mTORC1 as the upstream kinase of RagC on S21. ...
mTORC1 signalling promotes SREBP activation and lipogenesis in response to both physiological and genetic stimuli. In primary rodent hepatocytes and the intact liver, insulin or feeding has been shown to increase the expression of the major liver isoform of SREBP (SREBP1c) and its targets, and to promote de novo lipid synthesis in a manner that is sensitive to rapamycin [17,18,19]. Insulin activates mTORC1 through a pathway involving the Akt‐mediated phosphorylation and inhibition of TSC2, within a complex with TSC1 and TBC1D7 ]2,3,4]. Expression of constitutively active Akt or loss of either TSC1 or TSC2, both of which result in insulin‐independent activation of mTORC1 signalling, stimulates the global expression of SREBP1 and SREBP2 targets and drives lipogenesis through mTORC1 [15,16]. These latter studies found that mTORC1 signalling promotes accumulation of the processed, mature form of SREBP1, which resides in the nucleus to induce its own expression and that of genes involved in both ...
Mass spectrometry has proven to be a valuable tool for analyzing large protein complexes. This method enables insights into the...
The COP9 signalosome is a highly conserved protein complex composed of eight subunits. In this study a novel, regulatory mechanism of CSN biogenesis was identified. We used stable transfected siCSN1 cells in which the protein and the mRNA expression of CSN subuntis were downregulated. Transfection of His-CSN1 in those siCSN1 cells led to the induction of the de novo Synthesis of the whole CSN complex. In addition the expression of the transcription factors STAT1 and c-Myc was elevated. The cells were treated with IFN alpha or IFN gamma, respectively. This resulted in the induction of the CSN de novo synthesis. Moreover, the siRNA-mediated inhibition of STAT1, c-Myc, Lin28B as well as treatment with the pharmacological inhibitors AG9 or AG490 led to a reduced protein expression of the analysed CSN subunits. We found that in all experiments there was a significant change on protein level in contrast to a marginal change on the RNA level. Based on our study we hypothesized that the CSN biogenesis ...
Proline-rich AKT1 substrate 1 40 kDa (PRAS40) is a protein encoded by the AKT1S1 gene in humans. PRAS40 binds to 14-3-3 proteins when phosphorylated. PRAS40 is a subunit of the mammalian target of rapamycin complex 1 (mTORC1), and it negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. It inhibits RHEB-GTP-dependent mTORC1 activation. Although it is a substrate for AKT1 phosphorylation, PRAS40 can also be activated by AKT1-independent mechanisms. PRAS40 is also known as AKT1 substrate 1 (proline-rich), AKT1S1, proline-rich AKT1 substrate 1, lobe, and MGC2865.. ...
Proline-rich AKT1 substrate 1 40 kDa (PRAS40) is a protein encoded by the AKT1S1 gene in humans. PRAS40 binds to 14-3-3 proteins when phosphorylated. PRAS40 is a subunit of the mammalian target of rapamycin complex 1 (mTORC1), and it negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. It inhibits RHEB-GTP-dependent mTORC1 activation. Although it is a substrate for AKT1 phosphorylation, PRAS40 can also be activated by AKT1-independent mechanisms. PRAS40 is also known as AKT1 substrate 1 (proline-rich), AKT1S1, proline-rich AKT1 substrate 1, lobe, and MGC2865.. ...
The COP9 signalosome (CSN) is a conserved multiprotein complex, with an important developmental role in several organisms, ranging from plants to mammalians.
NYU Langone study suggests that placing strict biological controls on a portion of a protein complex could help stop a variety of cancers. Learn more.
part of a multiprotein complex, SRCAP-containing complex supporting ATP-dependent exchange of histone dimers containing H2B and H2AFZ into mononucleosomes reconstituted with recombinant H2A, H2B, H3, and H4 ...
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Nuclear fission, or nucleopore, is a large protein complex that passes through a nucleolem (a double membrane that encloses a nucleus in a e
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Gammons M, Bienz M (April 2018). "Multiprotein complexes governing Wnt signal transduction". Current Opinion in Cell Biology. ... The Dsh protein functions both in planar polarity and Wnt signalling, where it recruits another supramolecular complex (the ... An S, Kumar R, Sheets ED, Benkovic SJ (April 2008). "Reversible compartmentalization of de novo purine biosynthetic complexes ... Nakano A, Trie R, Tateishi K (January 1997). "Glycogen-Surfactant Complexes: Phase Behavior in a Water/Phytoglycogen/Sodium ...
"Baculovirus expression system for heterologous multiprotein complexes". Nature Biotechnology. 22 (12): 1583-1587. doi:10.1038/ ... Wenzel, Silke C; Müller, Rolf (2005-12-01). "Recent developments towards the heterologous expression of complex bacterial ... Through this host, it remains exceedingly challenging to heterologously express a complex, heteromultimeric metalloprotein like ...
Martinez E (December 2002). "Multi-protein complexes in eukaryotic gene transcription". Plant Molecular Biology. 50 (6): 925-47 ... Complex DNA and RNA organic compounds of life, including uracil, cytosine, and thymine, have also been formed in the laboratory ... The histones form a disk-shaped complex called a nucleosome, which contains two complete turns of double-stranded DNA wrapped ... In eukaryotes, this structure involves DNA binding to a complex of small basic proteins called histones, while in prokaryotes ...
Multiprotein complexes often form during caspase activation. Some activating multiprotein complexes includes: The death- ... This is done by the formation of a multiprotein Death Inducing Signalling Complex (DISC) that recruits and activates a pro- ... This cellular ion imbalance leads to oligomerisation of NLRP3 molecules to form a multiprotein complex called the NLRP3 ... These proteins allow caspase-1 activation by forming a multiprotein activating complex called Inflammasomes. For example, a NOD ...
"Baculovirus expression system for heterologous multiprotein complexes". Nature Biotechnology. 22 (12): 1583-1587. doi:10.1038/ ... His laborat-ory has elu-cidated the struc-tures of the nucle-osome core particle and vari-ous transcrip-tion factor complexes. ... particularly those involved in protein-DNA complexes and to relate these structures to the biological processes of chromatin ... in teach-ing and research are primar-ily devoted to the re-cog-ni-tion and assembly of biological macro-molecular complexes. X- ...
"Multi-Protein Complexes Involved in Cell Regulation (E6)". Keystone Symposia. 2006. Retrieved 24 October 2016. "Scientific ... has delivered several featured lectures and keynote addresses which included the Keystone Symposium on Multiprotein Complexes ( ... "Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the ...
Their interaction results in formation of multiprotein complexes. When Ets1 interacts with other transcription factors (Runx1, ... ETS1 binds with DNA-dependent protein kinase (DNA-PK) [where the DNA-PK complex is made up of DNA-PKcs and DNA repair Ku ( ...
Balbo A, Minor KH, Velikovsky CA, Mariuzza RA, Peterson CB, Schuck P (Jan 2005). "Studying multiprotein complexes by ... by either monitoring the number and molar mass of macromolecular complexes, by gaining information about the complex ... With AUC it is possible to gain information on the number and subunit stoichiometry of non-covalent complexes and equilibrium ...
... via their involvement in multiprotein complexes called inflammasomes. ENSG00000167634, ENSG00000278173, ENSG00000277179, ...
Most of genes are part of multi-protein complexes. This approach can be used to identify synthetic lethality by using the ... Complexes of proteins are allowed to form around a particular "bait" protein. The bait protein is identified using an antibody ... Vinayagam A, Hu Y, Kulkarni M, Roesel C, Sopko R, Mohr SE, Perrimon N (February 2013). "Protein complex-based analysis ... Affinity purification and mass spectrometry (AP/MS) is able to identify proteins that interact with one another in complexes. ...
"Acyl modification and binding of mitochondrial ACP to multiprotein complexes". Biochimica et Biophysica Acta (BBA) - Molecular ... A broad range of macromolecular complexes from CEF research areas A, C and D, including complex I, ATP synthase, drug ... Examples for important membrane complexes include the atomic structures of complex I and the ATP synthase of the mitochondrial ... Design of macromolecular complexes, and (E) Methods for studying macromolecular complexes. Biological membranes have a very ...
A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in ... The presence of this region in a number of other complex-forming proteins points to the possible involvement of the VWFC domain ... Fraser extracellular matrix complex subunit 1 (FRAS1) Neural EGFL like 1 (NELL1) Neural EGFL like 2 (NELL2) Peroxidasin like ( ... in complex formation. BMP binding endothelial regulator (BMPER) Cysteine-rich motor neuron 1 protein (CRIM1) Extracellular ...
A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWA domains participate in ...
Reaction centers are multi-protein complexes found within the thylakoid membrane. At the heart of a photosystem lies the ... Each photosystem has two main subunits: an antenna complex (a light harvesting complex or LHC) and a reaction center. The ... The antenna complex contains hundreds of chlorophyll molecules which funnel the excitation energy to the center of the ... Energy will be efficiently transferred from the outer part of the antenna complex to the inner part. This funneling of energy ...
Rodriguez P, Ruiz MT, Price GB, Zannis-Hadjopoulos M (2005). "NAP-2 is part of multi-protein complexes in HeLa cells". J. Cell ...
The CST complex is a cellular multiprotein complex involved in telomere maintenance. In budding yeast (Saccharomyces cerevisiae ... Sun J, Yu EY, Yang Y, Confer LA, Sun SH, Wan K, Lue NF, Lei M (December 2009). "Stn1-Ten1 is an Rpa2-Rpa3-like complex at ... It is related to the Replication protein A complex. For budding yeast as well as for mammals, CST is a protein heterotrimer, ... Lue NF, Zhou R, Chico L, Mao N, Steinberg-Neifach O, Ha T (2013). "The telomere capping complex CST has an unusual ...
Structural biology Nucleic acid quaternary structure Multiprotein complex Biomolecular complex Oligomers Here quaternary means ... Other assemblies referred to instead as multiprotein complexes also possess quaternary structure. Examples include nucleosomes ... In some cases, proteins form complexes that then assemble into even larger complexes. In such cases, one uses the nomenclature ... e.g., "dimer of dimers" or "trimer of dimers", to suggest that the complex might dissociate into smaller sub-complexes before ...
Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of ... "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332-42. doi: ... It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to ... Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to ...
LIM domain-containing proteins are scaffolds for the formation of multiprotein complexes. The proteins are involved in ... 2003). "A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels". Nat. Neurosci. 6 (5): 468-75. doi: ...
Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (2004). "A multiprotein trafficking complex composed of SAP97, ... "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium ... "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332-42. doi: ... Bohl J, Brimer N, Lyons C, Vande Pol SB (2007). "The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 ...
"The inner workings of the hydrazine synthase multiprotein complex". Nature. 527 (7578): 394-7. Bibcode:2015Natur.527..394D. doi ... At the same time, nitrite is reduced to hydroxylamine at the cytoplasmic site of the same enzyme complex responsible for ... In general, two possible reaction mechanisms are addressed: One mechanism hypothesizes that a membrane-bound enzyme complex ... ammonium and hydroxylamine are converted to hydrazine by a membrane-bound enzyme complex, hydrazine is oxidized in the ...
Bell SP, Stillman B (May 1992). "ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex ... First, the ORC, Noc3p and Cdc6 form a complex on origin DNA (marked by ARS type regions). New ORC/Noc3/Cdc6 complexes then ... Unlike eukaryotic Orc, they do not always form a complex. In fact, they have divergent complex structures when these do form. ... In molecular biology, origin recognition complex (ORC) is a multi-subunit DNA binding complex (6 subunits) that binds in all ...
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are ... Protein complex formation can activate or inhibit one or more of the complex members and in this way, protein complex formation ... Such protein complexes are called "obligate protein complexes". Transient protein complexes form and break down transiently in ... Proper assembly of multiprotein complexes is important, since misassembly can lead to disastrous consequences. In order to ...
... via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM] GRCh38: Ensembl ...
... via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM] GRCh38: Ensembl ...
"HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response". The Journal of Biological ... Huang J, Gong Z, Ghosal G, Chen J (August 2009). "SOSS complexes participate in the maintenance of genomic stability". ... "Streamlined analysis schema for high-throughput identification of endogenous protein complexes". Proceedings of the National ...
She is known for her work on multiprotein complexes involved in gene expression. and development of new supports for cryo-EM. ... Her group uses in vitro reconstitution, biochemical assays and cryo-EM to understand the function of multiprotein complexes ... She performed in vitro biochemical characterisation of the activity of the anaphase-promoting complex (APC) and used cryo-EM to ... Rajendra E, Garaycoechea JI, Patel KJ, Passmore LA (2014). "Abundance of the Fanconi anaemia core complex is regulated by the ...
Some of these transcription factors appear to form multi-protein DNA-bound complexes. Phosphorylation of the RHD appears to ...
Takayama Y, Kamimura Y, Okawa M, Muramatsu S, Sugino A, Araki H (2003). "GINS, a novel multiprotein complex required for ... DNA replication complex GINS protein PSF2 is a protein that in humans is encoded by the GINS2 gene. GINS2 has been shown to ... "Entrez Gene: GINS2 GINS complex subunit 2 (Psf2 homolog)". Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER, Hurov KE, Luo J ...
Hsp90 acts in a multiprotein complex with several co-chaperones. One of these, cochaperone p23, appears to stabilize Hsp90- ... Finally they concluded that Hsp90, and consequently signaling mediated by client proteins in the Hsp90 multiprotein complex, ... Geldanamycin and radicicol tightly bind to this pocket and prevent the release of protein from chaperone complex. Thus the ... Mitochondrial Hsp90 is involved in complex signaling pathway that prevents initiation of induced apoptosis. Gamitrinib is a ...
They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible ...
... a highly conserved multiprotein complex implicated in protein deneddylation, deubiquitination, and phosphorylation. RIG-G has ... Interferon type I: All type I IFNs bind to a specific cell surface receptor complex known as the IFN-α/β receptor (IFNAR) that ... As a result, an IFN-stimulated gene factor 3 (ISGF3) complex forms-this contains STAT1, STAT2 and a third transcription factor ... Interferon type III: Signal through a receptor complex consisting of IL10R2 (also called CRF2-4) and IFNLR1 (also called CRF2- ...
Most TPR-containing proteins are associated with multiprotein complexes, and there is extensive evidence indicating that TPR ... Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S (January 2011). "Structure of human O-GlcNAc transferase and its complex with a ... motifs are important to the functioning of chaperone, cell-cycle, transcription, and protein transport complexes. Two more TPR ...
... forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of ... Golas MM, Sander B, Will CL, Lührmann R, Stark H (May 2003). "Molecular architecture of the multiprotein splicing factor SF3b ... This gene encodes subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and ... Das BK, Xia L, Palandjian L, Gozani O, Chyung Y, Reed R (October 1999). "Characterization of a protein complex containing ...
... along with MIS12, DC8, PMF1, CBX5, ZWINT is a component of the kinetochore-associated multiprotein complex which is ... DSN1, MIND kinetochore complex component, homolog (S. cerevisiae), also known as DSN1 or MIS13, is a protein which in humans ... "Entrez Gene: DSN1 DSN1, MIND kinetochore complex component, homolog (S. cerevisiae)". Obuse C, Iwasaki O, Kiyomitsu T, Goshima ... 2004). "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1". Nat. Cell ...
Thereafter, one of the strands is incorporated into a multi-protein RNA-induced silencing complex (RISC). Among these proteins ... This complex is responsible for cleaving some of the hair-pin structures from the pre-microRNA which is transported to the ... Alternately, some SINEs are believed to use a much more complex system of integrating back into the genome; this system ... The chromosome has a very complex and hierarchical system of organizing the genome. This system of organization, which includes ...
Probiotics also help strengthen tight junctions, multiprotein complexes lining the intestines (as well as other organs and ...
Conserved oligomeric Golgi complex subunit 7 is a protein that in humans is encoded by the COG7 gene. Multiprotein complexes ... Several complexes have been identified, including the Golgi transport complex (GTC), the LDLC complex, which is involved in ... These 3 complexes are identical and have been termed the conserved oligomeric Golgi (COG) complex, which includes COG7 (Ungar ... Loh E, Hong W (2002). "Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi and exists in a complex with ...
"CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2 ... "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes". Biochem. Biophys. ... stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T ...
Adherens junctions, also called zonula adherens, are multiprotein complexes formed by proteins of the catenin and cadherin ... The molecular structure of this complex is in the form of a hexamer. The complex, which is embedded in the cell membranes of ... These complexes, formed primarily of members of the claudin and the occludin families, consist of about 35 different proteins, ... These complexes, consisting of transmembrane adhesion proteins of the cadherin family, link adjacent cells together through ...
Conserved oligomeric Golgi complex subunit 8 is a protein that in humans is encoded by the COG8 gene. Multiprotein complexes ... Several complexes have been identified, including the Golgi transport complex (GTC), the LDLC complex, which is involved in ... These 3 complexes are identical and have been termed the conserved oligomeric Golgi complex (COG), which includes COG8 (Ungar ... Whyte JR, Munro S (2001). "The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes ...
During her postdoctoral research, she worked on multi protein complexes of the translocase of the outer membrane. She ... complexes. By understanding these biological pathways, Koehler looks to better understand the dysfunction in mitochondria that ...
RNA polymerase II is then recruited to this multi-protein complex with the help of TFIIF. Additional transcription factors then ... TFIID first binds to the TATA box, facilitated by TFIIA binding to the upstream part of the TFIID complex. TFIIB then binds to ... When promoters use the SAGA/TATA box complex to recruit RNA polymerase II, they are more highly regulated and display higher ... Formation of the preinitiation complex begins when the multi-subunit transcription factor II D (TFIID) binds to the TATA box at ...
Action of histone deacetylase 1 and 2 (HDAC1/2) is induced by the interaction of mSin3A with a multi-protein complex containing ...
HATs are part of a multiprotein complex that is recruited to chromatin when activators bind to DNA binding sites. Acetylation ... The SWI/SNF protein complex in yeast is one example of a chromatin remodeling complex that regulates the expression of many ... In eukaryotes, genomic DNA is coiled into protein-DNA complexes called chromatin. Histones, which are the most prevalent type ... The nucleosome remodeling complexes reposition nucleosomes by several mechanisms, enabling or disabling accessibility of ...
Mediator is a multiprotein complex that functions as a transcriptional coactivator in all eukaryotes. It was discovered in 1990 ... Mediator complexes interact with transcription factors and RNA polymerase II. The main function of mediator complexes is to ... A more realistic model of a mediator complex without the CDK module is shown in the second figure. The mediator complex is ... the mediator complex undergoes a compositional change in which the kinase module dissociates from the complex to allow ...
Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm. Molecular reproduction and ... "Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm". Molecular Reproduction and ...
"Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex". Mol. Cell. 16 (5): 789-98 ... "Identification of a transcriptionally active peroxisome proliferator-activated receptor α-interacting cofactor complex in rat ...
... which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of ... WDR18 forms a nucleolar complex with LAS1L, PELP1, TEX10 called the rixosome which is involved in RNA degradation. The rixosome ... Recruitment of the rixosome by the Polycomb Repressive Complex 1 has been proposed to lead to its functioning in establishing ... Shipkovenska G, Durango A, Kalocsay M, Gygi SP, Moazed D (June 2020). "A conserved RNA degradation complex required for ...
... mutation occurs in two residues that are closely located in the tridimensional structure of the multi-protein complex. As thus ... Complex networks Gene therapy Suppressor mutation Synthetic lethality Motter, Adilson E; Gulbahce, Natali; Almaas, Eivind; ... A compensatory mutation in another component of the protein complex can then suppress the deleterious phenotype by re- ... Interaction-mediated suppression occurs when a deleterious mutation in a component of a protein complex destabilizes the ...
The physical role of the centromere is to act as the site of assembly of the kinetochores - a highly complex multiprotein ... are linked along their length by the action of the cohesin complex. It is now believed that this complex is mostly released ... The centromeric DNA is normally in a heterochromatin state, which is essential for the recruitment of the cohesin complex that ...
Gan B, Yoo Y, Guan JL (December 2006). "Association of focal adhesion kinase with tuberous sclerosis complex 2 in the ... FAK is typically located at structures known as focal adhesions, which are multi-protein structures that link the extracellular ... Schlaepfer DD, Broome MA, Hunter T (March 1997). "Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: ... "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". The Journal of ...
... may refer to: TRiC (complex), a multiprotein complex of eukaryotic cells involved in protein folding Tahoe Reno Industrial ...
Deoxyribonucleoproteins in this kind of complex interact to generate a multiprotein regulatory complex in which the intervening ... A deoxyribonucleoprotein (DNP) is a complex of DNA and protein. The prototypical examples are nucleosomes, complexes in which ... is a complex of ribonucleic acid and RNA-binding protein. These complexes play an integral part in a number of important ... Each RNP carries with it an RNA polymerase complex. When the nucleoprotein binds to the viral RNA, it is able to expose the ...
Many of these focal complexes fail to mature and are disassembled as the lamellipodia withdraw. However, some focal complexes ... Focal adhesions are integrin-containing, multi-protein structures that form mechanical links between intracellular actin ... Initially, small (0.25μm²) focal adhesions called focal complexes (FXs) are formed at the leading edge of the cell in ... Focal adhesions are large, dynamic protein complexes through which the cytoskeleton of a cell connects to the ECM. They are ...
... belong to a multiprotein complex. Some of the proteins which associates to the channel directly/indirectly include, but are not ... Anti-VGKC-complex encephalitis are caused by antibodies against the voltage gated potassium channel-complex (VGKC-complex) and ... VGKC-complex autoimmune encephalitis is an example of the latter form. Antibodies directed against VGKC were first reported in ... 2010). "Disruption of LGI1-linked synaptic complex causes abnormal synaptic transmission and epilepsy". Proc Natl Acad Sci U S ...
Multiprotein signalling complexes: regional assembly on heparan sulphate J.T. Gallagher J.T. Gallagher 1 ... J.T. Gallagher; Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans 1 June 2006; 34 (3 ... composite sulphated region, domain structure, fibroblast growth factor, heparan sulphate, K5 lyase, multiprotein signalling ... diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes ...
Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. In: ... Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. / Ardehali, ... Ardehali H, Chen Z, Ko Y, Mejía-Alvarez R, Marbán E. Multiprotein complex containing succinate dehydrogenase confers ... title = "Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity", ...
Multiprotein Complexes - Cyclin-Dependent Kinase 8 PubMed MeSh Term * Multiprotein Complexes - Mediator Complex Subunit 1 ... Multiprotein Complexes - Mediator Complex PubMed MeSh Term *Overview. Overview. subject area of * Activating RNAs associate ... The Mediator complex and transcription regulation Journal Article * The SCF-Fbw7 ubiquitin ligase degrades MED13 and MED13L and ... The human Mediator complex: a versatile, genome-wide regulator of transcription Journal Article ...
Multiprotein signalling complexes: regional assembly on heparan sulphate J.T. Gallagher J.T. Gallagher 1 ... J.T. Gallagher; Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans 1 June 2006; 34 (3 ... composite sulphated region, domain structure, fibroblast growth factor, heparan sulphate, K5 lyase, multiprotein signalling ... diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes ...
... *To: [email protected] ... Subject: [ccp4bb] Post-doctoral position in cryo-EM/structural biology of multiprotein signalling complexes ...
Multi-protein complexes at the beta-globin locus. Brief Funct Genomic Proteomic. 2006 Mar;5(1):62-5. doi: 10.1093/bfgp/ell001. ...
Multiprotein Complexes / metabolism * Mutation * Peptide Chain Initiation, Translational* * Phorbol Esters / pharmacology * ... which is then recruited into the complex in a phosphorylation-dependent manner. Thus, the eIF3 preinitiation complex acts as a ... We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a ... When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not. Cell stimulation promotes ...
Protein structure alignment and visualization of structural similarities; alignment of multiprotein complexes. Cα. Pair. No. ... "Detection of spatial correlations in protein structures and molecular complexes". Structure. 20 (4): 718-728. doi:10.1016/j. ...
mTOR kinases form 2 distinct multiprotein complexes, mTORC1 and mTORC2. In an in vitro and ex vivo study, 2 compounds, KU- ... Syed F, Sanganee HJ, Bahl A, Bayat A. Potent dual inhibitors of TORC1 and TORC2 complexes (KU-0063794 and KU-0068650) ...
... ... A multi‐protein complex from Myxococcus xanthus required for bacterial gliding motility Academic Article * ... In this study, we used biochemistry and cell biology analyses to identify multi-protein complexes associated with A-motility. ... These proteins, important for the correct localization of AgmU and AglZ, appear to be organized as a motility complex, spanning ...
In contrast, molecular details on lysosomal recruitment of the TSC complex have emerged only recently. The TSC complex subunit ... In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) ... In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) ... In this mini-review, we integrate the molecular mechanisms of lysosome and SG recruitment of the TSC complex. We discuss their ...
Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix ... The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind ... This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. ... explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. Kinetochores must interact ...
Multiprotein Complexes. 1. 2015. 1163. 0.090. Why? RNA, Viral. 1. 2017. 2842. 0.090. Why? ...
They found that these effects were mediated through the formation of a specific multiprotein complex comprising B-Raf, ... O. E. Pardo, C. Wellbrock, U. K. Khanzada et al., "FGF-2 protects small cell lung cancer cells from apoptosis through a complex ... Angiogenesis, which is the process by which new blood vessels develop from preexisting vessels, is governed by a very complex ... Heparin binds to bFGF and promotes the formation of ternary complexes with endothelial cell surface receptors, inducing an ...
However, methods suitable for screening multiprotein complexes (e.g. those composed of three or more different components) have ... Here, we explored an approach that uses reconstituted multiprotein complexes (RMPCs). As a model system, we chose heat shock ... High-throughput screen for inhibitors of protein-protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex ...
Here, we review techniques for map interpretation and provide examples from recent studies of multi-protein complexes. ... Electron cryo-microscopy (cryoEM) is used to determine structures of biological molecules, including multi-protein complexes. ... all-atom molecular dynamics simulations of the ribosome-tRNAs-mRNA-EFG complex were performed. The complex at the post- ... MDFF) to produce more accurate models of the ternary complex bound. to the ribosome (Trabuco et al., 2008; Villa et al., 2009 ...
1. Isolate membrane protein complexes by antibody purification: Best for identifying multiprotein complexes. ... 3. The complex nature of MS. Therefore, the top-down analyzes are limited to be applied to only low-throughput single-protein ... This allows the identification of protein rings and protein complex dissociation. Tandem Mass Spectrometry[edit , edit source] ... ESI-MS allows the study of the kinetics of protein complex assembly. Intermediates can be isolated as well as identified using ...
Proteomics of multiprotein complexes: answering fundamental questions in neuroscience. SGN Grant, H Husi ... Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. MO Collins ... Isolation of 2000‐kDa complexes of N‐methyl‐d‐aspartate receptor and postsynaptic density 95 from mouse brain. H Husi, SGN ... Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. H Husi, MA Ward, JS Choudhary, WP Blackstock, SGN ...
... design principles governing assembly of multiprotein complexes. Tomko Lab. ...
Visualization of the Genomic Loci That Are Bound by Specific Multiprotein Complexes by Bimolecular Fluorescence Complementation ...
... and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex ... This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA ... The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is ... Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to ...
Generation of branched actin networks: Assembly and regulation of WAVE and WASH multiprotein complexes Org.: Dr Thomas Falgui ... The multifunctional conserved p24 complex facilitates GPI-anchored protein transport, but how Org.: Prof. R. Watanabe ...
... site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex ... Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. They share the ability to domain ... Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. They share the ability to domain ... site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex ...
The SMC5/6 complex is previously described to promote DNA double-strand breaks (DSBs) repair by sister chromatid recombination ... Despite the essential nature of the SMC5/6 complex, the versatile mechanisms by which SMC5/6 functions and its molecular ... we found that the SMC5/6 complex physically interacts with the DNA topoisomerase II α (TOP2A). We therefore propose that the ... SMC5/6 complex functions in resolving TOP2A-mediated DSB-repair intermediates generated during replication. ...
This cytoplasmic, multi-protein complex responds to an array of different stressors but typically requires two signals. One ...
Our study points out the importance of the multiprotein complex for CoQ biosynthesis in mammals, which may provide new insights ... suggesting that the presence of a truncated version of COQ9 protein in Coq9R239X mice destabilizes the CoQ multiprotein complex ...
Damian C. Ekiert, PhD-how large multiprotein complexes transport lipids between membranes. Niels Ringstad, PhD-membrane ... Gregory David, PhD-the role of the Sin3 histone deacetylation complex in maintenance of genome integrity. Danny Reinberg, PhD- ... Karim-Jean Armache, PhD-structural approaches to study how gene-silencing complexes repress transcription. ...
Multiprotein Complexes [D05.500]. *Axin Signaling Complex [D05.500.117]. *Casein Kinase I [D05.500.117.750] ...
  • These proteins, important for the correct localization of AgmU and AglZ, appear to be organized as a motility complex, spanning the cytoplasm, inner membrane and the periplasm. (
  • Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. (
  • We show that these differences are due to the levels of COQ biosynthetic proteins, suggesting that the presence of a truncated version of COQ9 protein in Coq9R239X mice destabilizes the CoQ multiprotein complex. (
  • BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. (
  • CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins. (
  • Single copies of an alpha-helical-rich motif are demonstrated to be present within subunits of the large multiprotein 26S proteasome and eukaryotic initiation factor-3 (eIF3) complexes, and within proteins involved in transcriptional regulation. (
  • The presence of homologous, and sometimes identical, proteins in contrasting functional contexts suggests that the large multisubunit complexes of the 26S proteasome, eIF3 and TFIIH perform overlapping cellular roles. (
  • We found a fungal complex of seven proteins forming a structure with an essential role in disease development. (
  • Increased collagen II protein accumulation did not associate with increased col2a1 mRNA or a decrease in matrix metalloproteinase activity but, instead, it associated with increased expression of the endoplasmic reticulum/Golgi transport coat protein complex II Sec proteins. (
  • Polycystin 1 and polycystin 2 are multipass transmembrane proteins that function together as a receptor-ion channel complex, 1 leading to the widely held view that primary cellular defects in polycystin-deficient cells are caused by a disruption of normal Ca 2+ signaling. (
  • Although some Acr proteins against the Csy complex have been reported, other relevant Acr proteins still need studies to understand their mechanisms. (
  • As such, here, we obtain three structures of previously unresolved Acr proteins (AcrF9, AcrF8, and AcrF6) bound to the Csy complex using electron cryo-microscopy (cryo-EM), with resolution at 2.57 Å, 3.42 Å, and 3.15 Å, respectively. (
  • The 2.57-Å structure reveals fine details for each molecular component within the Csy complex as well as the direct and water-mediated interactions between proteins and CRISPR RNA (crRNA). (
  • Our structures also show unambiguously how these Acr proteins bind differently to the Csy complex. (
  • Acr proteins against the Csy complex. (
  • Our laboratory uses a genetic approach in mouse to discover genes, proteins and pathways that play an important role in complex human diseases. (
  • The presence of this region in a number of other complex-forming proteins points to the possible involvment of the VWFC domain in complex formation. (
  • The Myb proteins interact with a highly conserved multi-protein complex called the MuvB core. (
  • The same complex also interacts with proteins of the Rb tumor suppressor family and the E2F transcription factor family. (
  • My research goal is to use cryo-electron microscopy (cryo-EM) to determine the molecular structure of proteins and multi-protein complexes to understand their function. (
  • Proteins are complex molecules that play important functions in living organisms. (
  • Full-length Rb and MCM7 form protein complexes in vitro, and the amino termini of two Rb-related proteins, p107 and p130 , also bind MCM7 . (
  • The TSC complex subunit 1 (TSC1) binds lysosomes via phosphatidylinositol-3,5-bisphosphate [PI(3,5)P2]. (
  • Recent studies suggest that the pathogenesis of different inflammatory diseases also involves the inflammasomes, intracellular multiprotein complexes that mediate activation of inflammatory caspases thereby inducing the secretion of proinflammatory cytokines. (
  • Inflammasomes are multiprotein complexes and serve as platforms that mediate the release of innate cytokines after successful recognition, thereby attracting immune cells. (
  • Our study points out the importance of the multiprotein complex for CoQ biosynthesis in mammals, which may provide new insights to understand the genotype-phenotype heterogeneity associated with human CoQ deficiency and may have a potential impact on the treatment of this mitochondrial disorder. (
  • In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II. (
  • mTORC1 is an evolutionary highly conserved multi-protein complex. (
  • This cytoplasmic, multi-protein complex responds to an array of different stressors but typically requires two signals. (
  • The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold. (
  • Functions in a multi-protein complex in spermatid maturation. (
  • The new study, published in Proceedings of the National Academy of Sciences on March 5, has now shown that a multi-protein complex found in the body of P falciparum helps it convert haemoglobin into hemozoin. (
  • They identified a multi-protein complex, consisting of protease enzymes and haem detoxification protein, produced by the parasite. (
  • They found that this multi-protein complex is always present close to hemozoin crystals, suggesting it could have a role in crystal formation. (
  • This newly found pathway of hemozoin formation could be exploited to screen new anti-malarial drugs that could prevent the multi-protein complex from binding to haem and prevent subsequent hemozoin formation," says Malhotra. (
  • This effect is mediated through the formation of an apoptosome, a multi-protein complex consisting of cytochrome C, Apaf-1, pro-caspase 9 and ATP. (
  • The clustering of sulphated sugar residues in a series of complex domains with variable sulphation patterns generates considerable diversity in the molecular fine structure of HS. (
  • NGL viewer: web-based molecular graphics for large complexes. (
  • In contrast, molecular details on lysosomal recruitment of the TSC complex have emerged only recently. (
  • In this mini-review, we integrate the molecular mechanisms of lysosome and SG recruitment of the TSC complex. (
  • 5 ns) molecular dynamics simulations indicate that residues of Cks1 that form the binding site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex. (
  • Sensing of bacterial products by Naip5/Birc1e results in stimulation of a multiprotein complex known as the inflammasome that amplifies the molecular signal. (
  • Specific interactions - those that lead to formation of well-defined complexes consisting of exact molecular stoichiometries (e.g., protein-ligand complexes). (
  • CG-MALS is adept at characterizing both specific and non-specific interactions to determine the magnitude of the interaction and the true molecular stoichiometry (when applicable) of resultant complexes and oligomers. (
  • Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. (
  • The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA repair. (
  • Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. (
  • Comprehensive characterization of complex structural variations in cancer by directly comparing genome sequence reads. (
  • This equilibrium is concentration-dependent, so a fractionation technique such as SEC-MALS - with the accompanying time-dependent dilution - is not suitable for full and rigorous characterization of reversible complexes. (
  • We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a signal-dependent, choreographed fashion. (
  • Thus, the eIF3 preinitiation complex acts as a scaffold to coordinate a dynamic sequence of events in response to stimuli that promote efficient protein synthesis. (
  • This diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes on the HS polymer chain. (
  • Accordingly, it has been proposed that the Ska and Ndc80 complexes form an integrated MT-binding assembly 31 . (
  • Arginine dimethylation plays critical roles in the assembly of ribonucleoprotein complexes in pre-mRNA splicing and piRNA pathways. (
  • The tuberous sclerosis protein complex (TSC complex) is a key integrator of metabolic signals and cellular stress. (
  • Our results suggest that polycystin 2 deficiency causes increased collagen II synthesis with upregulation of secretory pathway coat protein complex II components. (
  • To confirm this, they inactivated falcipain-2, one of the protease enzymes in the protein complex, and observed if this hindered hemozoin formation. (
  • In addition, overexpression of KSR-1 in 293T cells leads to recruitment of MEK to a 700 kDa protein complex and translocates MEK from the soluble to the membrane-associated fraction. (
  • The ability of the Ska complex to track depolymerizing MTs in vitro and its dependency on the KMN for its localization and function suggest that the Ska complex may be a functional equivalent of the Dam/DASH complex in metazoans 25 , 26 . (
  • Reversible complexes are formed as a result of non-covalent interactions producing dynamic equilibrium between complexes and constituent monomers. (
  • Part of THO complex part of transcription export complex. (
  • Polymorphism of the THOC5 of the transcription/export multiprotein complex and its correlation with the lipid and metabolic profile in middle-aged women. (
  • RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. (
  • In this study, we used biochemistry and cell biology analyses to identify multi-protein complexes associated with A-motility. (
  • Cell stimulation promotes mTOR/raptor binding to the eIF3 complex and phosphorylation of S6K1 at its hydrophobic motif. (
  • When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not. (
  • Phosphorylation results in S6K1 dissociation, activation, and subsequent phosphorylation of its translational targets, including eIF4B, which is then recruited into the complex in a phosphorylation-dependent manner. (
  • In these research programs, we have cloned major genes that regulate response to infections, and in the case of complex genetic control, we have isolated single gene effects in unique recombinant or mutant mouse strains. (
  • This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. (
  • PACSAB: Coarse-Grained Force Field for the Study of Protein-Protein Interactions and Conformational Sampling in Multiprotein Systems. (
  • This is characteristic of MALDI-TOF mass spectrometry, which can determine the mass of individual components of large protein complexes. (
  • SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. (
  • Large T antigens of many polyomaviruses are able to form complexes with the retinoblastoma protein. (
  • The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. (
  • Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation. (
  • We discuss their interplay in the context of cell proliferation and migration in cancer and in the clinical manifestations of tuberous sclerosis complex disease (TSC) and lymphangioleiomyomatosis (LAM). (
  • This survival paradox has been attributed to a complex interplay between sociocultural and psychosocial factors, as well as other factors. (
  • The polycystin 1/2 complex in apical cilia participates in mechanosensory Ca 2+ signaling in response to fluid flow, 6 suggesting that loss of either polycystins or cilia structure would lead to acute loss of flow sensation and cyst formation. (
  • while they may lead to the formation of complexes or loosely-bound aggregates, these typically do not exhibit a well-defined stoichiometry or oligomeric state. (
  • The CALYPSO software offers an unparalleled set of association models with the flexibility to describe common as well as unusual complexes, all of which may be found in nature. (
  • Cells depleted of the Ska complex fail to maintain stable KT-MT attachments, resulting in chromosome congression failure followed by cell death 25 , 26 . (
  • In a mouse model of aerosol infection with Mycobacterium tuberculosis , we have shown that a locus on chromosome 7 is partly responsible for the complex genetic control of the inter-strain difference in susceptibility between C57BL/6J and DBA/2J. (
  • The PCI domain: a common theme in three multiprotein complexes. (
  • A common feature appears to be involvement in multiprotein complexes. (
  • We report solution structures of SMN and SPF30 Tudor domains bound to symmetric and asymmetric dimethylated arginine (DMA) that is inherent in the RNP complexes. (
  • Proteasomes come in a variety of flavors, and all are very complex multi-protein structures. (
  • Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. (
  • Here we report the crystal structure of superfamily 2 (SF2) ATPase domain of RIG-I in complex with a nucleotide analogue. (
  • Normally CAD exists as an inactive complex with ICAD (inhibitor of CAD). (
  • The TSC complex-mTORC1 axis translates nutrient and stress signals into tightly orchestrated cellular responses that impinge on anabolic processes including translation, as well as catabolic processes such as autophagy ( Liu and Sabatini, 2020 ). (
  • Angiogenesis, which is the process by which new blood vessels develop from preexisting vessels, is governed by a very complex network of opposing signals that, under normal physiological conditions, are elicited by various highly regulated angiogenesis stimulators and inhibitors [ 1 ]. (
  • Protein complexes between Rb and MCM7 were also detected in anti-Rb immunoprecipitates prepared from human cells. (