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Gene Review

REV1  -  REV1, polymerase (DNA directed)

Homo sapiens

Synonyms: AIBP80, Alpha integrin-binding protein 80, DNA repair protein REV1, REV1L, Rev1-like terminal deoxycytidyl transferase
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Disease relevance of REV1


High impact information on REV1

  • Rather, Rev1 is thought to contribute to mutagenesis principally by engaging in crucial protein-protein interactions that regulate the access of translesion DNA polymerases to the primer terminus [3].
  • Here, we report that S. cerevisiae Rev1 is subject to pronounced cell cycle control in which the levels of Rev1 protein are approximately 50-fold higher in G(2) and throughout mitosis than during G(1) and much of S phase [3].
  • Together with DNA polymerase zeta (Rev3/7), Rev1 function is required for the active introduction of the majority of mutations into the genomes of eukaryotes from yeast to humans [3].
  • However, the frequencies of 6-thioguanine resistance mutants induced by UV in the cells expressing antisense hREV1 RNA were significantly lower than in the control (P = 0.01), suggesting that the human gene has a function similar to that of the yeast homolog [4].
  • REV1 protein is a eukaryotic member of the Y family of DNA polymerases involved in the tolerance of DNA damage by replicative bypass [5].

Chemical compound and disease context of REV1


Biological context of REV1

  • Recently, the human REV1 (hREV1) and REV3 (hREV3) genes were identified, and their products were revealed to be involved in UV-induced mutagenesis, as observed for their yeast counterparts [7].
  • These findings suggest the possibility that hREV7 might play an important role in regulating the enzymatic activities of hREV1 and hREV3 for mutagenesis in response to DNA damage [7].
  • Determination of the chromosomal location of each SAM-identified gene revealed several locales within which genes lay in close proximity, including three genes (APACD, IF-2, and REV1L) located on chromosome 2 that lie immediately adjacent to each other and were significantly upregulated in three of five cell line pairs [8].
  • The rev1 mutator phenotype was specific for TNRs with hairpin forming capacity [9].
  • Furthermore, a mutant REV1 lacking N- and C-terminal domains, but catalytically active, lost this function, indicating that control is not due to the catalytic core [10].

Anatomical context of REV1

  • To further examine Poleta functions and the mechanisms that regulate this important protein, Poleta complexes were purified from HeLa cells over-expressing epitope-tagged Poleta, and polypeptides associated with Poleta, including Rad18, Rad6 and Rev1, were identified by a combination of mass spectrometry and Western blot analysis [11].
  • Affinity chromatography with these antibodies was used to isolate a single protein from Brucellergen and from B. melitensis cytosol preparations which produced a DTH reaction in guinea pigs sensitized with B. melitensis Rev1 [12].

Associations of REV1 with chemical compounds

  • Therefore, the molecular mechanism of the dCMP transfer reaction of the REV1S protein and maybe also the REV1 protein might be the same as that of the dNTP transfer reaction of the translesion DNA polymerases [13].
  • Human REV1 inserted a dCMP efficiently opposite a template 8-oxoguanine, (+)-trans-anti-benzo[a]pyrene-N2-dG, (-)-trans-anti-benzo[a]pyrene-N2-dG and 1,N6-ethenoadenine adducts, very inefficiently opposite an acetylaminofluorene-adducted guanine, but was unresponsive to a template TT dimer or TT (6-4) photoproduct [14].

Physical interactions of REV1

  • In this paper, we show that hREV1 interacts with hpol eta as well as with hpol kappa and poorly with hpol iota [15].

Other interactions of REV1

  • Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 [7].
  • These results suggest that arrested replication forks strengthen interactions among Poleta, Rad18/Rad6 and Rev1, consistent with the requirement for effective TLS by Poleta at sites of DNA lesions [11].
  • 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 [11].
  • In yeast, mutations induced by UV radiation are dependent on the function of the Rev1 gene product, a Y-family DNA polymerase that assists in translesion replication with potentially mutagenic consequences [16].

Analytical, diagnostic and therapeutic context of REV1


  1. Suppression of hREV1 expression reduces the rate at which human ovarian carcinoma cells acquire resistance to cisplatin. Okuda, T., Lin, X., Trang, J., Howell, S.B. Mol. Pharmacol. (2005) [Pubmed]
  2. Characterization of a monoclonal antibody specific for Brucella smooth lipopolysaccharide and development of a competitive enzyme-linked immunosorbent assay to improve the serological diagnosis of brucellosis. Weynants, V., Gilson, D., Cloeckaert, A., Denoel, P.A., Tibor, A., Thiange, P., Limet, J.N., Letesson, J.J. Clin. Diagn. Lab. Immunol. (1996) [Pubmed]
  3. The critical mutagenic translesion DNA polymerase Rev1 is highly expressed during G(2)/M phase rather than S phase. Waters, L.S., Walker, G.C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. Gibbs, P.E., Wang, X.D., Li, Z., McManus, T.P., McGregor, W.G., Lawrence, C.W., Maher, V.M. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  5. Ubiquitin-Binding Motifs in REV1 Protein Are Required for Its Role in the Tolerance of DNA Damage. Guo, C., Tang, T.S., Bienko, M., Parker, J.L., Bielen, A.B., Sonoda, E., Takeda, S., Ulrich, H.D., Dikic, I., Friedberg, E.C. Mol. Cell. Biol. (2006) [Pubmed]
  6. Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. Lin, X., Okuda, T., Trang, J., Howell, S.B. Mol. Pharmacol. (2006) [Pubmed]
  7. Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. Murakumo, Y., Ogura, Y., Ishii, H., Numata, S., Ichihara, M., Croce, C.M., Fishel, R., Takahashi, M. J. Biol. Chem. (2001) [Pubmed]
  8. cDNA microarray-based identification of genes and pathways associated with oxaliplatin resistance. Samimi, G., Manorek, G., Castel, R., Breaux, J.K., Cheng, T.C., Berry, C.C., Los, G., Howell, S.B. Cancer Chemother. Pharmacol. (2005) [Pubmed]
  9. Rev1 enhances CAG.CTG repeat stability in Saccharomyces cerevisiae. Collins, N.S., Bhattacharyya, S., Lahue, R.S. DNA Repair (Amst.) (2007) [Pubmed]
  10. Role of single-stranded DNA in targeting REV1 to primer termini. Masuda, Y., Kamiya, K. J. Biol. Chem. (2006) [Pubmed]
  11. 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. Yuasa, M.S., Masutani, C., Hirano, A., Cohn, M.A., Yamaizumi, M., Nakatani, Y., Hanaoka, F. Genes Cells (2006) [Pubmed]
  12. Brucella ribosomal protein L7/L12 is a major component in the antigenicity of brucellin INRA for delayed-type hypersensitivity in brucella-sensitized guinea pigs. Bachrach, G., Banai, M., Bardenstein, S., Hoida, G., Genizi, A., Bercovier, H. Infect. Immun. (1994) [Pubmed]
  13. Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. Masuda, Y., Takahashi, M., Tsunekuni, N., Minami, T., Sumii, M., Miyagawa, K., Kamiya, K. J. Biol. Chem. (2001) [Pubmed]
  14. Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion. Zhang, Y., Wu, X., Rechkoblit, O., Geacintov, N.E., Taylor, J.S., Wang, Z. Nucleic Acids Res. (2002) [Pubmed]
  15. Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. Tissier, A., Kannouche, P., Reck, M.P., Lehmann, A.R., Fuchs, R.P., Cordonnier, A. DNA Repair (Amst.) (2004) [Pubmed]
  16. Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. Clark, D.R., Zacharias, W., Panaitescu, L., McGregor, W.G. Nucleic Acids Res. (2003) [Pubmed]
  17. Interaction of hREV1 with three human Y-family DNA polymerases. Ohashi, E., Murakumo, Y., Kanjo, N., Akagi, J., Masutani, C., Hanaoka, F., Ohmori, H. Genes Cells (2004) [Pubmed]
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