Target type: biologicalprocess
The removal of covalent cross-link between DNA and a protein. [PMID:31921408]
Protein-DNA covalent cross-linking repair is a complex process that involves the removal of covalent adducts formed between proteins and DNA. These adducts can arise from various sources, including exposure to environmental toxins, cellular metabolism, and DNA damaging agents. The repair process is crucial for maintaining genomic integrity and preventing mutations that can lead to cancer and other diseases.
The first step in protein-DNA covalent cross-linking repair is the recognition of the damaged DNA. This recognition can be carried out by specialized DNA repair proteins, such as the nucleotide excision repair (NER) pathway proteins. Once the damaged DNA has been recognized, the next step is to remove the cross-linked protein. This can be achieved through various mechanisms, including proteolysis, where the protein is broken down into smaller fragments by proteases. Another mechanism is through the use of specialized DNA repair enzymes, such as tyrosyl-DNA phosphodiesterase 1 (TDP1), which can remove covalent cross-links between DNA and tyrosine residues.
Once the protein has been removed, the damaged DNA can be repaired. This repair process involves the removal of the damaged DNA sequence and its replacement with a new, undamaged sequence. This process is typically carried out by the NER pathway, which involves multiple steps, including incision, excision, and resynthesis of the damaged DNA.
Protein-DNA covalent cross-linking repair is a highly regulated process, involving a complex interplay of multiple proteins and enzymes. The efficiency of this repair process is crucial for maintaining genomic stability and preventing diseases. Mutations in the genes involved in this repair pathway can lead to increased susceptibility to cancer and other diseases.
The repair process is crucial for maintaining genomic integrity and preventing mutations that can lead to cancer and other diseases.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Fanconi anemia group J protein | A Fanconi anemia group J protein that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9BX63] | Homo sapiens (human) |
| Transitional endoplasmic reticulum ATPase | A transitional endoplasmic reticulum ATPase that is encoded in the genome of human. [PRO:DNx, UniProtKB:P55072] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| clotrimazole | conazole antifungal drug; imidazole antifungal drug; imidazoles; monochlorobenzenes | antiinfective agent; environmental contaminant; xenobiotic | |
| Telomestatin | 1,3-oxazoles | ||
| Methylenedioxycinnamic acid | hydroxycinnamic acid | ||
| 3,4-methylenedioxy-beta-nitrostyrene | 3,4-methylenedioxy-beta-nitrostyrene: tyrosine kinase inhibitor that prevents platelet glycoprotein IIb/IIIa activation; structure in first source | ||
| 4-(4-(4-chloro-phenyl)thiazol-2-ylamino)phenol | substituted aniline | ||
| ML240 | ML240 : A member of the class of quinazolines that is quinazoline which is substituted at positions 2, 5 and 8 by 2-amino-1H-benzimidazol-1-yl, benzylnitrilo and methoxy groups, respectively. It is a ATP-competetive inhibitor of AAA ATPase p97, also known as valosin-containing protein (VCP). | aromatic amine; aromatic ether; benzimidazoles; primary amino compound; quinazolines; secondary amino compound | antineoplastic agent |
| ganciclovir | 2-aminopurines; oxopurine | antiinfective agent; antiviral drug |