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Gene Review

Rev1  -  REV1 homolog (S. cerevisiae)

Mus musculus

Synonyms: 1110027I23Rik, AU022044, DNA repair protein REV1, REV1, Rev1-like terminal deoxycytidyl transferase, ...
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Disease relevance of Rev1

  • Efficacy of several antibiotic combinations against Brucella melitensis Rev 1 experimental infection in BALB/c mice [1].
  • CONCLUSIONS: Gentamicin may be used along with doxycycline when the classical combination is considered the first choice in the treatment of patients with brucellosis due to B. melitensis vaccine strain Rev 1 [1].

High impact information on Rev1

  • REV1 protein, a eukaryotic member of the Y family of DNA polymerases, is involved in the tolerance of DNA damage by translesion DNA synthesis [2].
  • In vivo studies in both chicken DT40 cells and yeast directly support the requirement of the BRCT domain of REV1 for cell survival and DNA damage-induced mutagenesis [2].
  • In addition, loss of Rev1 causes compensatory increase in mutagenesis by other translesion synthesis polymerases [3].
  • These results indicate that Rev1 incorporates deoxycytidine residues, most likely opposite abasic nucleotides, during somatic hypermutation [3].
  • Strand-biased defect in C/G transversions in hypermutating immunoglobulin genes in Rev1-deficient mice [3].

Chemical compound and disease context of Rev1

  • OBJECTIVES: The objective of the present study was to compare the efficacy of gentamicin given alone or combined with doxycycline with that of standard combination therapies in BALB/c mice experimentally infected with the Brucella melitensis vaccine strain Rev 1 [1].

Biological context of Rev1

  • Pol kappa and Rev1 are members of the Y family of DNA polymerases involved in tolerance to DNA damage by replicative bypass [translesion DNA synthesis (TLS)] [4].
  • In contrast, cell survival after MMS treatment is not reduced in the absence of REV1 [5].
  • We studied the effect of RNAi mediated down-regulation of the lesion bypass factor REV1 [5].
  • Together, these data indicate a regulatory role of the Rev1 BRCT domain in TLS of a limited spectrum of endogenous and exogenous nucleotide damages during a defined phase of the cell cycle [6].
  • In addition to its catalytic domain, Rev1 possesses a so-called BRCA1 C-terminal (BRCT) domain [6].

Anatomical context of Rev1

  • To better understand the role of lesion bypass polymerases in ICL repair, we investigated recombination-independent repair of ICLs in REV3 and REV1 deletion mutants constructed in avian DT40 cells and mouse embryonic fibroblast cells [7].
  • Although Rev1-/- mice display transient growth retardation, proliferation of Rev1-/- LPS-stimulated B cells is indistinguishable from wild-type cells [3].
  • The steady-state level of REV1 protein was reduced by more than 95% using stable expression of a siRNA construct in a Pol beta null cell line [5].

Associations of Rev1 with chemical compounds

  • Notwithstanding the physical interaction between Rev1 and Pol kappa, the DNA polymerase activity of each measured by primer extension in vitro is unaffected by the complex, either when extending normal primer-termini, when bypassing a single thymine glycol lesion, or when extending certain mismatched primer termini [4].
  • Here we show, by using the yeast two-hybrid assay and the glutathione S-transferase pull-down assay, that mouse REV1 can physically interact with ubiquitin [8].
  • Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein [9].
  • Furthermore, it could be established that the mouse Rev1 protein inserts dGMP and dTMP residues opposite template guanine at a V(max) similar to that for dCMP [9].
  • Recombinant mouse Rev1 protein was found to insert a dCMP residue opposite guanine, adenine, thymine, cytosine, uracil, and an apurinic/apyrimidinic site and to have weak ability for transfer to a mismatched terminus [9].

Regulatory relationships of Rev1


  1. Efficacy of several antibiotic combinations against Brucella melitensis Rev 1 experimental infection in BALB/c mice. Grilló, M.J., De Miguel, M.J., Muñoz, P.M., Marín, C.M., Ariza, J., Blasco, J.M. J. Antimicrob. Chemother. (2006) [Pubmed]
  2. REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo. Guo, C., Sonoda, E., Tang, T.S., Parker, J.L., Bielen, A.B., Takeda, S., Ulrich, H.D., Friedberg, E.C. Mol. Cell (2006) [Pubmed]
  3. Strand-biased defect in C/G transversions in hypermutating immunoglobulin genes in Rev1-deficient mice. Jansen, J.G., Langerak, P., Tsaalbi-Shtylik, A., van den Berk, P., Jacobs, H., de Wind, N. J. Exp. Med. (2006) [Pubmed]
  4. Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. Guo, C., Fischhaber, P.L., Luk-Paszyc, M.J., Masuda, Y., Zhou, J., Kamiya, K., Kisker, C., Friedberg, E.C. EMBO J. (2003) [Pubmed]
  5. REV1 mediated mutagenesis in base excision repair deficient mouse fibroblast. Poltoratsky, V., Horton, J.K., Prasad, R., Wilson, S.H. DNA Repair (Amst.) (2005) [Pubmed]
  6. The BRCT domain of mammalian Rev1 is involved in regulating DNA translesion synthesis. Jansen, J.G., Tsaalbi-Shtylik, A., Langerak, P., Calléja, F., Meijers, C.M., Jacobs, H., de Wind, N. Nucleic Acids Res. (2005) [Pubmed]
  7. REV3 and REV1 play major roles in recombination-independent repair of DNA interstrand cross-links mediated by monoubiquitinated proliferating cell nuclear antigen (PCNA). Shen, X., Jun, S., O'Neal, L.E., Sonoda, E., Bemark, M., Sale, J.E., Li, L. J. Biol. Chem. (2006) [Pubmed]
  8. 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]
  9. Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein. Masuda, Y., Takahashi, M., Fukuda, S., Sumii, M., Kamiya, K. J. Biol. Chem. (2002) [Pubmed]
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