Target type: molecularfunction
Binding to C-rich, single-stranded DNA. [PMID:8127654]
C-rich single-stranded DNA (ssDNA) binding is a crucial molecular function involved in a variety of cellular processes. C-rich ssDNA regions often serve as binding sites for specific proteins, facilitating diverse interactions and regulatory mechanisms. The binding process is characterized by the recognition of cytosine-rich sequences within ssDNA, driven by interactions between specific amino acid residues in the protein and the exposed bases of the DNA. These interactions can involve hydrogen bonding, electrostatic interactions, and hydrophobic interactions.
C-rich ssDNA binding proteins play significant roles in several key cellular functions, including:
1. DNA replication: During DNA replication, C-rich ssDNA regions can act as binding sites for proteins involved in unwinding the double helix and stabilizing the replication fork. These proteins prevent the reannealing of the separated strands, facilitating the efficient synthesis of new DNA.
2. DNA repair: C-rich ssDNA regions can also be involved in DNA repair mechanisms. Proteins that bind to these regions can help identify damaged DNA segments, recruit repair enzymes, and facilitate the repair process.
3. Gene regulation: C-rich ssDNA regions often occur in regulatory elements of genes, such as promoters and enhancers. The binding of proteins to these regions can influence gene expression by modulating transcription factor binding, chromatin structure, and other regulatory mechanisms.
4. Telomere maintenance: Telomeres, the protective caps at the ends of chromosomes, are composed of C-rich ssDNA sequences. C-rich ssDNA binding proteins are essential for maintaining telomere integrity, preventing chromosome degradation, and ensuring proper cell division.
5. Viral replication: Certain viruses utilize C-rich ssDNA binding proteins for their replication. These proteins can bind to viral DNA, facilitating the transcription and translation of viral genes, leading to the production of new viral particles.
The molecular function of C-rich ssDNA binding is highly specific and varies depending on the protein involved. Different proteins exhibit distinct binding affinities, sequence preferences, and functional roles. The detailed characterization of these binding interactions is crucial for understanding the complex regulatory networks within cells and for developing therapeutic strategies targeting specific DNA-protein interactions.'
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Protein | Definition | Taxonomy |
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Inosine-5'-monophosphate dehydrogenase | An inosine-5-monophosphate dehydrogenase that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P0ADG7] | Escherichia coli K-12 |
Compound | Definition | Classes | Roles |
---|---|---|---|
adenosine monophosphate | Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position. | adenosine 5'-phosphate; purine ribonucleoside 5'-monophosphate | adenosine A1 receptor agonist; cofactor; EC 3.1.3.1 (alkaline phosphatase) inhibitor; EC 3.1.3.11 (fructose-bisphosphatase) inhibitor; fundamental metabolite; micronutrient; nutraceutical |
inosinic acid | Inosine Monophosphate: Inosine 5'-Monophosphate. A purine nucleotide which has hypoxanthine as the base and one phosphate group esterified to the sugar moiety. | inosine phosphate; purine ribonucleoside 5'-monophosphate | Escherichia coli metabolite; human metabolite; mouse metabolite |