Function
DNA repair proteins correct DNA damage caused by mutations or toxins[1].
- DNA repair protein Rad4 is a yeast protein involved in DNA damage recognition in nucleotide excision repair[2]. Rad4 is an ortholog of the XPC protein. Rad4 opens up damaged DNA by inserting β-hairpin into the duplex and flipping out two damage-containing nucleotide pairs[3].
- DNA repair protein Rev1 is a DNA polymerase active in DNA damage sites. It contains 2 ubiquitin-binding sites[4].
- DNA repair protein Rad23A, DNA repair protein Rad23B isee UV excision repair protein.
- DNA repair protein Rad51 is a multifunctional protein with a role in DNA replication, homologous recombination repair and immunity[5].
- DNA repair protein Xrcc1 interacts with components of single-strand DNA breaks repair in mammalian cells[6].
- DNA repair protein Xrcc4 interacts with components of double-strand DNA breaks repair in mammalian cells[7].
- DNA repair protein PprA or Pleiotropic protein promoting DNA repair A facilitates the radiation resistance of Deinococcus radiodurans[8].
Relevance
DNA repair protein Rad51 is a potential marker for DNA repair in solid malignancies[9].
Disease
Mutations in DNA repair protein Rad4 can cause the xeroderma pigmentosum skin cancer predisposition syndrome[10].
Structural highlights
(PDB entry 2qsg). inserts into DNA making hydrogen bond interactions as well as non-bonding interactions with it[11]. .
3D Structures of DNA repair protein
DNA repair protein 3D structures
References
- ↑ Tainer JA, Thayer MM, Cunningham RP. DNA repair proteins. Curr Opin Struct Biol. 1995 Feb;5(1):20-6. PMID:7773744 doi:10.1016/0959-440x(95)80005-l
- ↑ den Dulk B, Brandsma JA, Brouwer J. The Rad4 homologue YDR314C is essential for strand-specific repair of RNA polymerase I-transcribed rDNA in Saccharomyces cerevisiae. Mol Microbiol. 2005 Jun;56(6):1518-26. doi: 10.1111/j.1365-2958.2005.04607.x. PMID:15916602 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.04607.x
- ↑ Velmurugu Y, Chen X, Slogoff Sevilla P, Min JH, Ansari A. Twist-open mechanism of DNA damage recognition by the Rad4/XPC nucleotide excision repair complex. Proc Natl Acad Sci U S A. 2016 Apr 19;113(16):E2296-305. doi:, 10.1073/pnas.1514666113. Epub 2016 Mar 31. PMID:27035942 doi:http://dx.doi.org/10.1073/pnas.1514666113
- ↑ Cui G, Botuyan MV, Mer G. Structural Basis for the Interaction of Mutasome Assembly Factor REV1 with Ubiquitin. J Mol Biol. 2018 Jul 6;430(14):2042-2050. doi: 10.1016/j.jmb.2018.05.017. Epub, 2018 May 18. PMID:29778604 doi:http://dx.doi.org/10.1016/j.jmb.2018.05.017
- ↑ Bhattacharya S, Srinivasan K, Abdisalaam S, Su F, Raj P, Dozmorov I, Mishra R, Wakeland EK, Ghose S, Mukherjee S, Asaithamby A. RAD51 interconnects between DNA replication, DNA repair and immunity. Nucleic Acids Res. 2017 May 5;45(8):4590-4605. PMID:28334891 doi:10.1093/nar/gkx126
- ↑ Caldecott KW. XRCC1 protein; Form and function. DNA Repair (Amst). 2019 Sep;81:102664. PMID:31324530 doi:10.1016/j.dnarep.2019.102664
- ↑ Critchlow SE, Bowater RP, Jackson SP. Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Curr Biol. 1997 Aug 1;7(8):588-98. PMID:9259561 doi:10.1016/s0960-9822(06)00258-2
- ↑ Adachi M, Shimizu R, Shibazaki C, Satoh K, Fujiwara S, Arai S, Narumi I, Kuroki R. Extended structure of pleiotropic DNA repair-promoting protein PprA from Deinococcus radiodurans. FASEB J. 2018 Nov 27:fj201801506R. doi: 10.1096/fj.201801506R. PMID:30481062 doi:http://dx.doi.org/10.1096/fj.201801506R
- ↑ Gachechiladze M, Škarda J, Soltermann A, Joerger M. RAD51 as a potential surrogate marker for DNA repair capacity in solid malignancies. Int J Cancer. 2017 Oct 1;141(7):1286-1294. PMID:28477336 doi:10.1002/ijc.30764
- ↑ Min JH, Pavletich NP. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature. 2007 Oct 4;449(7162):570-5. Epub 2007 Sep 19. PMID:17882165 doi:10.1038/nature06155
- ↑ Min JH, Pavletich NP. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature. 2007 Oct 4;449(7162):570-5. Epub 2007 Sep 19. PMID:17882165 doi:10.1038/nature06155
