Nuclear Respiratory Factor 1
Nuclear Respiratory Factors
NF-E2-Related Factor 1
GA-Binding Protein Transcription Factor
Mitochondrial Turnover
DNA, Mitochondrial
Electron Transport Complex IV
Mitochondrial Proteins
Transcription Factors
Trans-Activators
Promoter Regions, Genetic
Mitochondria
DNA-Binding Proteins
Base Sequence
Molecular Sequence Data
Transcription, Genetic
HeLa Cells
Gene Expression Regulation
Binding Sites
RNA, Messenger
Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells. (1/77)
Nuclear respiratory factor (NRF)-1 appears to be important for the expression of several respiratory genes, but there is no direct evidence that NRF-1 transduces a physiological signal into the production of an enzyme critical for mitochondrial biogenesis. We generated HeLa cells containing plasmids allowing doxycycline-inducible expression of uncoupling protein (UCP)-1. In the absence of doxycycline, UCP-1 mRNA and protein were undetectable. In the presence of doxycycline, UCP-1 was expressed and oxygen consumption doubled. This rise in oxygen consumption was associated with an increase in NRF-1 mRNA. It was also associated with an increase in NRF-1 protein binding activity as determined by electrophoretic mobility shift assay using a functional NRF-1 binding site from the delta-aminolevulinate (ALA) synthase promoter. Respiratory uncoupling also caused a time-dependent increase in protein levels of ALA synthase, an early marker for mitochondrial biogenesis. ALA synthase induction by respiratory uncoupling was prevented by transfecting cells with an oligonucleotide antisense to the region of the NRF-1 initiation codon; a scrambled oligonucleotide with the same base composition had no effect. Respiratory uncoupling increases oxygen consumption and lowers energy reserves. In HeLa cells, uncoupling also increases ALA synthase, an enzyme critical for mitochondrial respiration, but only if translatable mRNA for NRF-1 is available. These data suggest that the transcription factor NRF-1 plays a key role in cellular adaptation to energy demands by translating physiological signals into an increased capacity for generating energy. (+info)Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. (2/77)
Mitochondrial number and function are altered in response to external stimuli in eukaryotes. While several transcription/replication factors directly regulate mitochondrial genes, the coordination of these factors into a program responsive to the environment is not understood. We show here that PGC-1, a cold-inducible coactivator of nuclear receptors, stimulates mitochondrial biogenesis and respiration in muscle cells through an induction of uncoupling protein 2 (UCP-2) and through regulation of the nuclear respiratory factors (NRFs). PGC-1 stimulates a powerful induction of NRF-1 and NRF-2 gene expression; in addition, PGC-1 binds to and coactivates the transcriptional function of NRF-1 on the promoter for mitochondrial transcription factor A (mtTFA), a direct regulator of mitochondrial DNA replication/transcription. These data elucidate a pathway that directly links external physiological stimuli to the regulation of mitochondrial biogenesis and function. (+info)Activation of PPARgamma coactivator-1 through transcription factor docking. (3/77)
Transcriptional coactivators have been viewed as constitutively active components, using transcription factors mainly to localize their functions. Here, it is shown that PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 (SRC-1) and CREB binding protein (CBP)/p300. PGC-1 has a low inherent transcriptional activity when it is not bound to a transcription factor. The docking of PGC-1 to peroxisome proliferator-activated receptor gamma (PPARgamma) stimulates an apparent conformational change in PGC-1 that permits binding of SRC-1 and CBP/p300, resulting in a large increase in transcriptional activity. Thus, transcription factor docking switches on the activity of a coactivator protein. (+info)The CNC basic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents. Role for Nrf1 in gamma-gcs(l) and gss expression in mouse fibroblasts. (4/77)
Nrf1 is a member of the CNC-basic leucine zipper (CNC-bZIP) family of transcription factors. CNC bZIP factors, together with small Maf proteins, bind as heterodimers to the NF-E2/AP-1 element. Similarity between the NF-E2/AP-1 element and the antioxidant response element identified in a number of promoters of genes involved in detoxification and antioxidant response raises the possibility that Nrf1 plays a role in mediating the antioxidant response element response. In this study, we exploited the availability of cells from Nrf1 knockout mice to study the role of Nrf1 transcription factor in the regulation of antioxidant gene expression and in cellular antioxidant response. Fibroblast cells derived from Nrf1 null embryos showed lower levels of glutathione and enhanced sensitivity to the toxic effects of oxidant compounds. Our results indicate that Nrf1 plays a role in the regulation of genes involved in glutathione synthesis and suggest a basis for a correspondingly low GSH concentration and reduced stress response. (+info)Structural basis for the regulation of UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase-3 gene expression in adenocarcinoma cells. (5/77)
The UDP-N-acetyl-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyl transferase-3 (Gal NAc-T3) gene, a member of the Gal NAc transferase gene family, is expressed in a tissue-specific manner. To elucidate the function of this gene, we have focused on the molecular mechanism underlying regulation of gene expression. We have cloned Gal NAc-T3 cDNA and used it to show that Gal NAc-T3 mRNA is expressed in tumor cell lines derived from secretory epithelial tissue adenocarcinomas but not in cell lines derived from bladder and epidermoid carcinomas. Using a polyclonal antibody to Gal NAc-T3, we observed protein expression in adenocarcinoma but not non-adenocarcinoma cell lines, and in breast carcinoma cells but not in normal breast tissue. We used Gal NAc-T3 cDNA to isolate three overlapping genomic clones containing the 5'-portion of the human Gal NAc-T3 gene, and we sequenced 1.6 kb around the first exon. A transient expression assay using the luciferase gene showed that promoter activity was much higher in MCF-7 cells than in KB cells. In vivo footprint experiments showed significant protection of a distal GC box, an NRF-1 site, and an AP-2 site in MCF-7 cells. A novel stem and loop structure extending from nucleotide -103 to nucleotide -165 and contiguous to these transcription factor binding sites seemed to be functional in regulating Gal NAc-T3 gene transcription, and a KMnO4 footprint experiment showed that this stem and loop structure could be formed in vivo. We also observed dimethyl sulfate hypersensitive sites in the untranslated region around nucleotide +50 in MCF-7 but not in KB cells. These findings indicate that Gal NAc-T3 gene expression is regulated by multiple systems, including transcription factor binding sites and a stem-and-loop structure, and that this regulation is restricted to cell lines derived from epithelial gland adenocarcinomas but not cells derived from nonsecretory epithelial tissue carcinomas. In addition, our immunohistochemical results suggest that our anti-Gal NAc-T3 antibody may be useful for diagnostic purposes in the early stages of breast cancer. (+info)Antagonism between members of the CNC-bZIP family and the immediate-early protein IE2 of human cytomegalovirus. (6/77)
The HCMV IE2 protein negatively autoregulates its own expression as well as represses the transactivation activity of p53. Using the repression domain of IE2 as bait in the yeast two-hybrid system, Nrf1 and Nrf2, members of the CNC-bZIP family, were found to be IE2-interacting proteins. Residues 331-448 encompassing the DNA-binding and the dimerization domains of Nrf1 are sufficient for the interaction. The interaction was further confirmed in vitro by a glutathione S-transferase pull-down assay and in vivo by co-immunoprecipitation. In transient transfection studies, transcription driven by six copies of an NF-E2 site or by chimeric proteins between the DNA-binding domain of LexA and members of the CNC-bZIP family is repressed by IE2. Importantly, the DNA binding activity of the Nrf1/MafK heterodimer is not impeded by IE2. In a parallel study, CNC-bZIP factors attenuate the negative autoregulation of IE2. The attenuation could be explained by the finding that Nrf1 functions alone and synergistically with its heterodimerization partner, MafK, in inhibiting the DNA binding activity of IE2. Taken together, these results demonstrate the existence of antagonism between members of the CNC-bZIP family and IE2. (+info)Identification of a nuclear respiratory factor-1 binding site within the core promoter of the human polio virus receptor/CD155 gene. (7/77)
In this report we describe a cis-acting element within the core promoter of the CD155 gene specifying the polio virus receptor that is bound by the nuclear respiratory factor-1 (NRF-1) transcription factor. DNase I footprint analysis identified a nuclear protein binding site from -282 to -264 nucleotides upstream of the translation initiation codon of the CD155 gene, which we have called foot print IV (FPIV). Linker scanning mutagenesis revealed that a tandem repeat motif, GCGCAGGCGCAG, located within FPIV was essential for the basal activity of the CD155 core promoter. The results of the electrophoretic mobility shift assay experiments suggested that identical FPIV binding activities were present in a variety of nuclear extracts and that the tandem repeat was essential for binding. A one-hybrid screen was then carried out using FPIV as bait to clone the cDNA of the FPIV binding factor. The sequences of the cDNAs that were cloned from the screen were identical to NRF-1, a result that was confirmed by further electrophoretic mobility shift assay experiments. Overexpression of full-length NRF-1 and a dominant-negative form of NRF-1 modulated reporter gene expression driven by the core promoter. Remarkably, CD155 is the first gene shown to be regulated by NRF-1 that possesses an expression profile during embryogenesis correlating with this factor's proposed role in the development of the vertebrate optic system. We propose that NRF-1, which has been shown by others to be expressed during embryogenesis in animal systems, may be involved in regulating the expression of CD155 at specific stages of central nervous system development. (+info)Sequential serum-dependent activation of CREB and NRF-1 leads to enhanced mitochondrial respiration through the induction of cytochrome c. (8/77)
Progression through the cell cycle requires ATP for protein synthesis, cytoskeletal rearrangement, chromatin remodeling, and protein degradation. The mechanisms by which mammalian cells increase respiratory capacity and ATP production in preparation for cell division are largely unexplored. Here, we demonstrate that serum induction of cytochrome c mRNA and processed protein in quiescent BALB/3T3 fibroblasts is associated with a marked increase in mitochondrial respiration. Cytochrome c was induced in the absence of any increase in citrate synthase activity or in subunit IV of the cytochrome c oxidase complex mRNA or protein, indicating that the enhanced respiratory rate did not require a general increase in mitochondrial biogenesis or respiratory chain expression. Transfections with a series of cytochrome c promoter mutants showed that both nuclear respiratory factor 1 (NRF-1) and cAMP-response element-binding protein (CREB) binding sites contributed equally to induced expression by serum. Moreover, CREB and NRF-1 were phosphorylated sequentially in response to serum, and the NRF-1 phosphorylation was accompanied by an increase in its ability to trans-activate target gene expression. The results demonstrate that the differential transcriptional expression of cytochrome c, through sequential transcription factor phosphorylations, leads to enhanced mitochondrial respiratory capacity upon serum-induced entry to the cell cycle. (+info)Nuclear Respiratory Factor 1 (NRF-1) is a transcription factor that plays a crucial role in the regulation of genes involved in nuclear and mitochondrial respiratory chain function, as well as in the biogenesis of mitochondria. It is a member of the Cap'n'Collar (CNC) family of basic region-leucine zipper (bZIP) transcription factors. NRF-1 regulates the expression of genes encoding subunits of complexes I, III, IV, and V of the electron transport chain, as well as enzymes involved in heme and iron-sulfur cluster biosynthesis. It also plays a role in the regulation of cellular antioxidant response by regulating the expression of genes encoding antioxidant enzymes such as superoxide dismutase and glutathione peroxidase. NRF-1 is widely expressed in various tissues, including the heart, brain, liver, and skeletal muscle.
Nuclear respiratory factors (NRFs) are a family of transcription factors that play crucial roles in the regulation of mitochondrial biogenesis and function. They are involved in the expression of genes encoding for proteins required for oxidative phosphorylation, the electron transport chain, and the tricarboxylic acid cycle (TCA cycle).
There are two main types of NRFs: NRF-1 and NRF-2. Both of these factors bind to specific DNA sequences called antioxidant response elements (AREs) in the promoter regions of their target genes, thereby activating their transcription.
NRF-1 is involved in the regulation of both nuclear and mitochondrial genes that are required for oxidative phosphorylation and other mitochondrial functions. It also plays a role in the biogenesis of mitochondria by regulating the expression of proteins involved in mitochondrial DNA replication, transcription, and translation.
NRF-2 is primarily involved in the regulation of antioxidant response genes that protect cells from oxidative stress. However, it also plays a role in mitochondrial biogenesis by regulating the expression of proteins involved in mitochondrial respiration and metabolism.
Overall, NRFs are essential for maintaining mitochondrial function and cellular homeostasis, and their dysregulation has been implicated in various diseases, including neurodegenerative disorders, cancer, and metabolic diseases.
Nuclear factor, erythroid-derived 2, like 1 (NFE2L1), also known as NF-E2-related factor 1 (NRF1), is a protein involved in the regulation of genes that protect cells against oxidative stress and damage. It encodes a basic leucine zipper (bZIP) transcription factor that binds to antioxidant response elements (AREs) in the promoter regions of target genes, leading to their activation and increased expression. NRF1 plays a crucial role in maintaining cellular redox homeostasis and protecting against various stressors, including chemicals, radiation, and inflammation. Mutations in the NFE2L1 gene have been associated with several diseases, such as neurodegenerative disorders and cancer.
A GA-binding protein (GABP) transcription factor is a type of protein complex that regulates gene expression by binding to specific DNA sequences known as GATA motifs. These motifs contain the consensus sequence (T/A)GAT(A/G)(A/T). GABP is composed of two subunits, GABPα and GABPβ, which form a heterodimer that recognizes and binds to the GATA motif.
GABP plays a crucial role in various biological processes, including cell proliferation, differentiation, and survival. It is involved in the regulation of genes that are important for the function of the cardiovascular, respiratory, and immune systems. Mutations in the genes encoding GABP subunits have been associated with several human diseases, such as congenital heart defects, pulmonary hypertension, and immunodeficiency disorders.
Overall, GABP transcription factors are essential regulators of gene expression that play a critical role in maintaining normal physiological functions and homeostasis in the body.
I'm sorry for any confusion, but "mitochondrial turnover" is not a widely recognized or established medical term with a specific definition. Mitochondria are the powerhouses of the cell, responsible for producing energy in the form of ATP through a process called oxidative phosphorylation.
The term "turnover," when used in a biological context, generally refers to the process by which cells replace or regenerate their components over time. Therefore, one might infer that "mitochondrial turnover" could refer to the replacement and regeneration of mitochondria within cells. However, this is not a standardized term, and its precise meaning could vary depending on the context.
Mitochondria are known to undergo dynamic processes such as fusion (combining) and fission (dividing), which allow them to change their size, shape, and distribution in response to cellular needs. Additionally, damaged or dysfunctional mitochondria can be removed through a process called mitophagy, where they're targeted for degradation within lysosomes. New, healthy mitochondria are generated through biogenesis, which involves the production of new mitochondrial proteins and membranes.
In summary, while "mitochondrial turnover" is not a standard medical term, it could be used to describe the ongoing processes of mitochondrial dynamics, mitophagy, and biogenesis that contribute to the replacement and regeneration of mitochondria within cells over time.
Mitochondrial DNA (mtDNA) is the genetic material present in the mitochondria, which are specialized structures within cells that generate energy. Unlike nuclear DNA, which is present in the cell nucleus and inherited from both parents, mtDNA is inherited solely from the mother.
MtDNA is a circular molecule that contains 37 genes, including 13 genes that encode for proteins involved in oxidative phosphorylation, a process that generates energy in the form of ATP. The remaining genes encode for rRNAs and tRNAs, which are necessary for protein synthesis within the mitochondria.
Mutations in mtDNA can lead to a variety of genetic disorders, including mitochondrial diseases, which can affect any organ system in the body. These mutations can also be used in forensic science to identify individuals and establish biological relationships.
Electron Transport Complex IV is also known as Cytochrome c oxidase. It is the last complex in the electron transport chain, located in the inner mitochondrial membrane of eukaryotic cells and the plasma membrane of prokaryotic cells. This complex contains 13 subunits, two heme groups (a and a3), and three copper centers (A, B, and C).
In the electron transport chain, Complex IV receives electrons from cytochrome c and transfers them to molecular oxygen, reducing it to water. This process is accompanied by the pumping of protons across the membrane, contributing to the generation of a proton gradient that drives ATP synthesis via ATP synthase (Complex V). The overall reaction catalyzed by Complex IV can be summarized as follows:
4e- + 4H+ + O2 → 2H2O
Defects in Cytochrome c oxidase can lead to various diseases, including mitochondrial encephalomyopathies and neurodegenerative disorders.
Mitochondrial proteins are any proteins that are encoded by the nuclear genome or mitochondrial genome and are located within the mitochondria, an organelle found in eukaryotic cells. These proteins play crucial roles in various cellular processes including energy production, metabolism of lipids, amino acids, and steroids, regulation of calcium homeostasis, and programmed cell death or apoptosis.
Mitochondrial proteins can be classified into two main categories based on their origin:
1. Nuclear-encoded mitochondrial proteins (NEMPs): These are proteins that are encoded by genes located in the nucleus, synthesized in the cytoplasm, and then imported into the mitochondria through specific import pathways. NEMPs make up about 99% of all mitochondrial proteins and are involved in various functions such as oxidative phosphorylation, tricarboxylic acid (TCA) cycle, fatty acid oxidation, and mitochondrial dynamics.
2. Mitochondrial DNA-encoded proteins (MEPs): These are proteins that are encoded by the mitochondrial genome, synthesized within the mitochondria, and play essential roles in the electron transport chain (ETC), a key component of oxidative phosphorylation. The human mitochondrial genome encodes only 13 proteins, all of which are subunits of complexes I, III, IV, and V of the ETC.
Defects in mitochondrial proteins can lead to various mitochondrial disorders, which often manifest as neurological, muscular, or metabolic symptoms due to impaired energy production. These disorders are usually caused by mutations in either nuclear or mitochondrial genes that encode mitochondrial proteins.
Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.
Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.
In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.
Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.
Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).
Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.
DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.
The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.
DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.
A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.
During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.
Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.
HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.
HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.
It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.
'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.