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*{{cite journal |vauthors=Gibbs PE, Wang XD, Li Z, etal |title=The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4186–91 |year= 2000 |pmid= 10760286 |doi=10.1073/pnas.97.8.4186 | pmc=18191 }}
*{{cite journal | author=Wixler V, Geerts D, Laplantine E, et al. |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669–78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 }}
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*{{cite journal | author=Masuda Y, Takahashi M, Tsunekuni N, et al. |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051–8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 }}
*{{cite journal |vauthors=Masuda Y, Takahashi M, Tsunekuni N, etal |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051–8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 }}
*{{cite journal | author=Murakumo Y, Ogura Y, Ishii H, et al. |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644–51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 }}
*{{cite journal |vauthors=Murakumo Y, Ogura Y, Ishii H, etal |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644–51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, et al. |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356–60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 }}
*{{cite journal | author=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356–60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 }}
*{{cite journal | author=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981–8 |year= 2004 |pmid= 12930947 |doi=10.1093/nar/gkg725 | pmc=212819 }}
*{{cite journal | author=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981–8 |year= 2004 |pmid= 12930947 |doi=10.1093/nar/gkg725 | pmc=212819 }}
*{{cite journal | author=Guo C, Fischhaber PL, Luk-Paszyc MJ, et al. |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621–30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626 | pmc=291821 }}
*{{cite journal |vauthors=Guo C, Fischhaber PL, Luk-Paszyc MJ, etal |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621–30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626 | pmc=291821 }}
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*{{cite journal | author=Lin X, Okuda T, Trang J, Howell SB |title=Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. |journal=Mol. Pharmacol. |volume=69 |issue= 5 |pages= 1748–54 |year= 2006 |pmid= 16495473 |doi= 10.1124/mol.105.020446 }}
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*{{cite journal | author=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314–21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 }}
*{{cite journal | author=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314–21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 }}
*{{cite journal | author=Yuasa MS, Masutani C, Hirano A, et al. |title=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. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731–44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x }}
*{{cite journal |vauthors=Yuasa MS, Masutani C, Hirano A, etal |title=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. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731–44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x }}
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Revision as of 02:02, 2 September 2015

Template:PBB DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.[1][2] Template:PBB Summary 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[by whom?] 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 ζ (Rev3/Rev7).

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 ζ (Rev3/Rev7) a B family polymerase involved in TLS.

References

  1. ^ 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): 4468–75. doi:10.1093/nar/27.22.4468. PMC 148731. PMID 10536157.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ "Entrez Gene: REV1 REV1 homolog (S. cerevisiae)".
  3. ^ Nair, DT (Sep 30, 2005). "Rev1 employs a novel mechanism of DNA synthesis using a protein template". Science. doi:10.1126/science.1116336. PMID 16195463. Retrieved Feb 6, 2015.
  4. ^ 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. 276 (38). United States: 35644–51. doi:10.1074/jbc.M102051200. ISSN 0021-9258. PMID 11485998. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)CS1 maint: unflagged free DOI (link)

Further reading

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