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REV1
Introduction
DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.[1][2] This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.[2] Rev1 is a Y family DNA polymerase; it is sometimes referred to as a deoxycytidyl transferase because it only inserts deoxycytidine (dC) across from lesions. Whether G, A, T, C, or an abasic site, Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an arginine as a template which complements well with C.[3] Yet it is believed that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1’s primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ΞΆ (Rev3/Rev7).
Interactions
Interactions
REV1 has been shown to interact with MAD2L2.[4] It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ΞΆ (Rev3/Rev7) a B family polymerase involved in TLS.
References
References
- β Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z (Dec 1999). “The human REV1 gene codes for a DNA template-dependent dCMP transferase”. Nucleic Acids Res. 27 (22): 4468β75. doi:10.1093/nar/27.22.4468. PMCΒ 148731. PMIDΒ 10536157.
- β 2.0 2.1 “Entrez Gene: REV1 REV1 homolog (S. cerevisiae)”.
- β Nair, DT (Sep 30, 2005). “Rev1 employs a novel mechanism of DNA synthesis using a protein template”. Science. 309: 2219β22. Bibcode:2005Sci…309.2219N. doi:10.1126/science.1116336. PMIDΒ 16195463.
- β Murakumo, Y; Ogura Y; Ishii H; Numata S; Ichihara M; Croce C M; Fishel R; Takahashi M (September 2001). “Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7”. J. Biol. Chem. United States. 276 (38): 35644β51. doi:10.1074/jbc.M102051200. ISSNΒ 0021-9258. PMIDΒ 11485998.
Further reading
Further reading
- Bonaldo MF, Lennon G, Soares MB (1997). “Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Res. 6 (9): 791β806. doi:10.1101/gr.6.9.791. PMIDΒ 8889548.
- Wixler V, Laplantine E, Geerts D, et al. (1999). “Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains”. FEBS Lett. 445 (2β3): 351β5. doi:10.1016/S0014-5793(99)00151-9. PMIDΒ 10094488.
- Gibbs PE, Wang XD, Li Z, et al. (2000). “The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light”. Proc. Natl. Acad. Sci. U.S.A. 97 (8): 4186β91. Bibcode:2000PNAS…97.4186G. doi:10.1073/pnas.97.8.4186. PMCΒ 18191. PMIDΒ 10760286.
- Wixler V, Geerts D, Laplantine E, et al. (2000). “The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes”. J. Biol. Chem. 275 (43): 33669β78. doi:10.1074/jbc.M002519200. PMIDΒ 10906324.
- Masuda Y, Takahashi M, Tsunekuni N, et al. (2001). “Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain”. J. Biol. Chem. 276 (18): 15051β8. doi:10.1074/jbc.M008082200. PMIDΒ 11278384.
- Murakumo Y, Ogura Y, Ishii H, et al. (2001). “Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7”. J. Biol. Chem. 276 (38): 35644β51. doi:10.1074/jbc.M102051200. PMIDΒ 11485998.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899β903. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMCΒ 139241. PMIDΒ 12477932.
- Masuda Y, Ohmae M, Masuda K, Kamiya K (2003). “Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins”. J. Biol. Chem. 278 (14): 12356β60. doi:10.1074/jbc.M211765200. PMIDΒ 12529368.
- Clark DR, Zacharias W, Panaitescu L, McGregor WG (2004). “Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene”. Nucleic Acids Res. 31 (17): 4981β8. doi:10.1093/nar/gkg725. PMCΒ 212819. PMIDΒ 12930947.
- Guo C, Fischhaber PL, Luk-Paszyc MJ, et al. (2004). “Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis”. EMBO J. 22 (24): 6621β30. doi:10.1093/emboj/cdg626. PMCΒ 291821. PMIDΒ 14657033.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40β5. doi:10.1038/ng1285. PMIDΒ 14702039.
- Ohashi E, Murakumo Y, Kanjo N, et al. (2005). “Interaction of hREV1 with three human Y-family DNA polymerases”. Genes Cells. 9 (6): 523β31. doi:10.1111/j.1356-9597.2004.00747.x. PMIDΒ 15189446.
- Tissier A, Kannouche P, Reck MP, et al. (2005). “Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein”. DNA Repair (Amst.). 3 (11): 1503β14. doi:10.1016/j.dnarep.2004.06.015. PMIDΒ 15380106.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). “Generation and annotation of the DNA sequences of human chromosomes 2 and 4”. Nature. 434 (7034): 724β31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMIDΒ 15815621.
- Lin X, Okuda T, Trang J, Howell SB (2006). “Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells”. Mol. Pharmacol. 69 (5): 1748β54. doi:10.1124/mol.105.020446. PMIDΒ 16495473.
- Masuda Y, Kamiya K (2006). “Role of single-stranded DNA in targeting REV1 to primer termini”. J. Biol. Chem. 281 (34): 24314β21. doi:10.1074/jbc.M602967200. PMIDΒ 16803901.
- Yuasa MS, Masutani C, Hirano A, et al. (2006). “A human DNA polymerase eta complex containing Rad18, Rad6 and Rev1; proteomic analysis and targeting of the complex to the chromatin-bound fraction of cells undergoing replication fork arrest”. Genes Cells. 11 (7): 731β44. doi:10.1111/j.1365-2443.2006.00974.x. PMIDΒ 16824193.
