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Volumn 287, Issue 12, 2012, Pages 9613-9622

The vital role of polymerase ζ and REV1 in mutagenic, but not correct, DNA synthesis across Benzo[a]pyrene-dG and recruitment of polymerase ζ by REV1 to replication-stalled site

Author keywords

[No Author keywords available]

Indexed keywords

BENZO [A] PYRENE; C TERMINUS; CATALYTIC SUBUNITS; COMPLEX PROCESSES; DNA LESIONS; DNA SYNTHESISS; MAMMALIAN CELLS; MISCODING FREQUENCY; MOUSE EMBRYONIC FIBROBLASTS; TRANSLESION SYNTHESIS; WILD TYPES;

EID: 84858608663     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331728     Document Type: Article
Times cited : (41)

References (48)
  • 3
    • 77953921670 scopus 로고    scopus 로고
    • Structural basis for the suppression of skin cancers by DNA polymerase ε
    • Silverstein, T. D., Johnson, R. E., Jain, R., Prakash, L., Prakash, S., and Aggarwal, A. K. (2010) Structural basis for the suppression of skin cancers by DNA polymerase ε. Nature 465, 1039-1043
    • (2010) Nature , vol.465 , pp. 1039-1043
    • Silverstein, T.D.1    Johnson, R.E.2    Jain, R.3    Prakash, L.4    Prakash, S.5    Aggarwal, A.K.6
  • 6
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum
    • DOI 10.1126/science.285.5425.263
    • Johnson, R. E., Kondratick, C. M., Prakash, S., and Prakash, L. (1999) hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 285, 263-265 (Pubitemid 29330001)
    • (1999) Science , vol.285 , Issue.5425 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 8
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • DOI 10.1038/382729a0
    • Nelson, J. R., Lawrence, C. W., and Hinkle, D. C. (1996) Deoxycytidyl transferase activity of yeast REV1 protein. Nature 382, 729-731 (Pubitemid 26282181)
    • (1996) Nature , vol.382 , Issue.6593 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 9
    • 0033571521 scopus 로고    scopus 로고
    • The human REV1 gene codes for a DNA template-dependent dCMP transferase
    • DOI 10.1093/nar/27.22.4468
    • Lin, W., Xin, H., Zhang, Y., Wu, X., Yuan, F., and Wang, Z. (1999) The human REV1 gene codes for a DNA template-dependent dCMP transferase. Nucleic Acids Res. 27, 4468-4475 (Pubitemid 29533189)
    • (1999) Nucleic Acids Research , vol.27 , Issue.22 , pp. 4468-4475
    • Lin, W.1    Xin, H.2    Zhang, Y.3    Wu, X.4    Yuan, F.5    Wang, Z.6
  • 10
    • 77956102849 scopus 로고    scopus 로고
    • The catalytic function of the Rev1 dCMP transferase is required in a lesion-specific manner for translesion synthesis and base damage-induced mutagenesis
    • Zhou, Y., Wang, J., Zhang, Y., and Wang, Z. (2010) The catalytic function of the Rev1 dCMP transferase is required in a lesion-specific manner for translesion synthesis and base damage-induced mutagenesis. Nucleic Acids Res. 38, 5036-5046
    • (2010) Nucleic Acids Res. , vol.38 , pp. 5036-5046
    • Zhou, Y.1    Wang, J.2    Zhang, Y.3    Wang, Z.4
  • 11
    • 78951481539 scopus 로고    scopus 로고
    • The DNA polymerase activity of Saccharomyces cerevisiae Rev1 is biologically significant
    • Wiltrout, M. E., and Walker, G. C. (2011) The DNA polymerase activity of Saccharomyces cerevisiae Rev1 is biologically significant. Genetics 187, 21-35
    • (2011) Genetics , vol.187 , pp. 21-35
    • Wiltrout, M.E.1    Walker, G.C.2
  • 12
    • 14844362615 scopus 로고    scopus 로고
    • Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1
    • DOI 10.1093/nar/gki279
    • Ross, A. L., Simpson, L. J., and Sale, J. E. (2005) Vertebrate DNA damage tolerance requires the C-terminus but not BRCT or transferase domains of REV1. Nucleic Acids Res. 33, 1280-1289 (Pubitemid 41439921)
    • (2005) Nucleic Acids Research , vol.33 , Issue.4 , pp. 1280-1289
    • Ross, A.-L.1    Simpson, L.J.2    Sale, J.E.3
  • 13
    • 0345732688 scopus 로고    scopus 로고
    • Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis
    • DOI 10.1093/emboj/cdg626
    • Guo, C., Fischhaber, P. L., Luk-Paszyc, M. J., Masuda, Y., Zhou, J., Kamiya, K., Kisker, C., and Friedberg, E. C. (2003) Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. EMBO J. 22, 6621-6630 (Pubitemid 38009608)
    • (2003) EMBO Journal , vol.22 , Issue.24 , pp. 6621-6630
    • Guo, C.1    Fischhaber, P.L.2    Luk-Paszyc, M.J.3    Masuda, Y.4    Zhou, J.5    Kamiya, K.6    Kisker, C.7    Friedberg, E.C.8
  • 14
    • 3042812439 scopus 로고    scopus 로고
    • Interaction of hREV1 with three human Y-family DNA polymerases
    • DOI 10.1111/j.1356-9597.2004.00747.x
    • Ohashi, E., Murakumo, Y., Kanjo, N., Akagi, J., Masutani, C., Hanaoka, F., and Ohmori, H. (2004) Interaction of hREV1 with three human Y-family DNA polymerases. Genes Cells 9, 523-531 (Pubitemid 38877782)
    • (2004) Genes to Cells , vol.9 , Issue.6 , pp. 523-531
    • Ohashi, E.1    Murakumo, Y.2    Kanjo, N.3    Akagi, J.-I.4    Masutani, C.5    Hanaoka, F.6    Ohmori, H.7
  • 16
    • 0038823615 scopus 로고    scopus 로고
    • Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins
    • DOI 10.1074/jbc.M211765200
    • Masuda, Y., Ohmae, M., Masuda, K., and Kamiya, K. (2003) Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. J. Biol. Chem. 278, 12356-12360 (Pubitemid 36800219)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12356-12360
    • Masuda, Y.1    Ohmae, M.2    Masuda, K.3    Kamiya, K.4
  • 17
    • 60549092109 scopus 로고    scopus 로고
    • Bypass specialists operate together
    • Takata, K., and Wood, R. D. (2009) Bypass specialists operate together. EMBO J. 28, 313-314
    • (2009) EMBO J. , vol.28 , pp. 313-314
    • Takata, K.1    Wood, R.D.2
  • 19
    • 10044266718 scopus 로고    scopus 로고
    • Cellular functions of DNA polymerase zeta and Rev1 protein
    • Lawrence, C. W. (2004) Cellular functions of DNA polymerase zeta and Rev1 protein. Adv. Protein Chem. 69, 167-203
    • (2004) Adv. Protein Chem. , vol.69 , pp. 167-203
    • Lawrence, C.W.1
  • 22
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • DOI 10.1038/nature00991
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (Pubitemid 35025438)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 23
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • DOI 10.1038/nature01965
    • Stelter, P., and Ulrich, H. D. (2003) Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-191 (Pubitemid 37150898)
    • (2003) Nature , vol.425 , Issue.6954 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 24
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase ε with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage
    • DOI 10.1016/S1097-2765(04)00259-X, PII S109727650400259X
    • Kannouche, P. L., Wing, J., and Lehmann, A. R. (2004) Interaction of human DNA polymerase ε with monoubiquitinated PCNA. A possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14, 491-500 (Pubitemid 38648802)
    • (2004) Molecular Cell , vol.14 , Issue.4 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 26
    • 43449133259 scopus 로고    scopus 로고
    • PCNA Ubiquitination and REV1 Define Temporally Distinct Mechanisms for Controlling Translesion Synthesis in the Avian Cell Line DT40
    • DOI 10.1016/j.molcel.2008.03.024, PII S1097276508003249
    • Edmunds, C. E., Simpson, L. J., and Sale, J. E. (2008) PCNA ubiquitination and REV1 define temporally distinct mechanisms for controlling translesion synthesis in the avian cell line DT40. Mol. Cell 30, 519-529 (Pubitemid 351672376)
    • (2008) Molecular Cell , vol.30 , Issue.4 , pp. 519-529
    • Edmunds, C.E.1    Simpson, L.J.2    Sale, J.E.3
  • 29
    • 0037125136 scopus 로고    scopus 로고
    • Activities of human DNA polymerase κ in response to the major benzo[a]pyrene DNA adduct: Error-free lesion bypass and extension synthesis from opposite the lesion
    • DOI 10.1016/S1568-7864(02)00055-1, PII S1568786402000551
    • Zhang, Y., Wu, X., Guo, D., Rechkoblit, O., and Wang, Z. (2002) Activities of human DNA polymerase κ in response to the major benzo[a]pyrene DNA adduct. Error-free lesion bypass and extension synthesis from opposite the lesion. DNA Repair 1, 559-569 (Pubitemid 34655713)
    • (2002) DNA Repair , vol.1 , Issue.7 , pp. 559-569
    • Zhang, Y.1    Wu, X.2    Guo, D.3    Rechkoblit, O.4    Wang, Z.5
  • 30
    • 58649116940 scopus 로고    scopus 로고
    • Two distinct translesion synthesis pathways across a lipid peroxidation-derived DNA adduct in mammalian cells
    • Yang, I. Y., Hashimoto, K., de Wind, N., Blair, I. A., and Moriya, M. (2009) Two distinct translesion synthesis pathways across a lipid peroxidation-derived DNA adduct in mammalian cells. J. Biol. Chem. 284, 191-198
    • (2009) J. Biol. Chem. , vol.284 , pp. 191-198
    • Yang, I.Y.1    Hashimoto, K.2    De Wind, N.3    Blair, I.A.4    Moriya, M.5
  • 31
    • 6344288785 scopus 로고    scopus 로고
    • Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • DOI 10.1038/sj.emboj.7600383
    • Watanabe, K., Tateishi, S., Kawasuji, M., Tsurimoto, T., Inoue, H., and Yamaizumi, M. (2004) Rad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J. 23, 3886-3896 (Pubitemid 39389719)
    • (2004) EMBO Journal , vol.23 , Issue.19 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3    Tsurimoto, T.4    Inoue, H.5    Yamaizumi, M.6
  • 35
    • 0030466095 scopus 로고    scopus 로고
    • Fidelity of translesional synthesis past benzo[a]pyrene diol epoxide-2′-deoxyguanosine DNA adducts. Marked effects of host cell, sequence context, and chirality
    • Moriya, M., Spiegel, S., Fernandes, A., Amin, S., Liu, T., Geacintov, N., and Grollman, A. P. (1996) Fidelity of translesional synthesis past benzo[a]pyrene diol epoxide-2′-deoxyguanosine DNA adducts. Marked effects of host cell, sequence context, and chirality. Biochemistry 35, 16646-16651
    • (1996) Biochemistry , vol.35 , pp. 16646-16651
    • Moriya, M.1    Spiegel, S.2    Fernandes, A.3    Amin, S.4    Liu, T.5    Geacintov, N.6    Grollman, A.P.7
  • 36
    • 0014202537 scopus 로고
    • Selective extraction of polyoma DNA from infected mouse cell cultures
    • Hirt, B. (1967) Selective extraction of polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 26, 365-369
    • (1967) J. Mol. Biol. , vol.26 , pp. 365-369
    • Hirt, B.1
  • 37
    • 33748654795 scopus 로고    scopus 로고
    • Translesion DNA synthesis across the heptanone-etheno-2′- deoxycytidine adduct in cells
    • DOI 10.1021/tx0600503
    • Pollack, M., Yang, I. Y., Kim, H. Y., Blair, I. A., and Moriya, M. (2006) Translesion DNA synthesis across the heptanone-etheno-2′-deoxycytidine adduct in cells. Chem. Res. Toxicol. 19, 1074-1079 (Pubitemid 44384838)
    • (2006) Chemical Research in Toxicology , vol.19 , Issue.8 , pp. 1074-1079
    • Pollack, M.1    Yang, I.-Y.2    Kim, H.-Y.H.3    Blair, I.A.4    Moriya, M.5
  • 40
    • 0033859845 scopus 로고    scopus 로고
    • Evidence for a second function for Saccharomyces cerevisiae Rev1p
    • DOI 10.1046/j.1365-2958.2000.01997.x
    • Nelson, J. R., Gibbs, P. E., Nowicka, A. M., Hinkle, D. C., and Lawrence, C. W. (2000) Evidence for a second function for Saccharomyces cerevisiae Rev1p. Mol. Microbiol. 37, 549-554 (Pubitemid 30611835)
    • (2000) Molecular Microbiology , vol.37 , Issue.3 , pp. 549-554
    • Nelson, J.R.1    Gibbs, P.E.M.2    Nowicka, A.M.3    Hinkle, D.C.4    Lawrence, C.W.5
  • 41
    • 77951218269 scopus 로고    scopus 로고
    • Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase ζ and REV1
    • Hara, K., Hashimoto, H., Murakumo, Y., Kobayashi, S., Kogame, T., Unzai, S., Akashi, S., Takeda, S., Shimizu, T., and Sato, M. (2010) Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase ζ and REV1. J. Biol. Chem. 285, 12299-12307
    • (2010) J. Biol. Chem. , vol.285 , pp. 12299-12307
    • Hara, K.1    Hashimoto, H.2    Murakumo, Y.3    Kobayashi, S.4    Kogame, T.5    Unzai, S.6    Akashi, S.7    Takeda, S.8    Shimizu, T.9    Sato, M.10
  • 42
    • 48149104225 scopus 로고    scopus 로고
    • Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance
    • D'Souza, S., Waters, L. S., and Walker, G. C. (2008) Novel conserved motifs in Rev1 C-terminus are required for mutagenic DNA damage tolerance. DNA Repair 7, 1455-1470
    • (2008) DNA Repair , vol.7 , pp. 1455-1470
    • D'Souza, S.1    Waters, L.S.2    Walker, G.C.3
  • 43
    • 33746162368 scopus 로고    scopus 로고
    • REV1 Protein Interacts with PCNA: Significance of the REV1 BRCT Domain In Vitro and In Vivo
    • DOI 10.1016/j.molcel.2006.05.038, PII S1097276506003807
    • Guo, C., Sonoda, E., Tang, T. S., Parker, J. L., Bielen, A. B., Takeda, S., Ulrich, H. D., and Friedberg, E. C. (2006) REV1 protein interacts with PCNA. Significance of the REV1 BRCT domain in vitro and in vivo. Mol. Cell 23, 265-271 (Pubitemid 44081878)
    • (2006) Molecular Cell , vol.23 , Issue.2 , pp. 265-271
    • Guo, C.1    Sonoda, E.2    Tang, T.-S.3    Parker, J.L.4    Bielen, A.B.5    Takeda, S.6    Ulrich, H.D.7    Friedberg, E.C.8
  • 45
    • 79959906411 scopus 로고    scopus 로고
    • Sequential assembly of translesion DNA polymerases at UV-induced DNA damage sites
    • Andersen, P. L., Xu, F., Ziola, B., McGregor, W. G., and Xiao, W. (2011) Sequential assembly of translesion DNA polymerases at UV-induced DNA damage sites. Mol. Biol. Cell 22, 2373-2383
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2373-2383
    • Andersen, P.L.1    Xu, F.2    Ziola, B.3    McGregor, W.G.4    Xiao, W.5
  • 46
    • 80053044268 scopus 로고    scopus 로고
    • The non-canonical protein binding site at the monomer-monomer interface of yeast proliferating cell nuclear antigen (PCNA) regulates the Rev1-PCNA interaction and Polζ/Rev1-dependent translesion DNA synthesis
    • Sharma, N. M., Kochenova, O. V., and Shcherbakova, P. V. (2011) The non-canonical protein binding site at the monomer-monomer interface of yeast proliferating cell nuclear antigen (PCNA) regulates the Rev1-PCNA interaction and Polζ/Rev1-dependent translesion DNA synthesis. J. Biol. Chem. 286, 33557-33566
    • (2011) J. Biol. Chem. , vol.286 , pp. 33557-33566
    • Sharma, N.M.1    Kochenova, O.V.2    Shcherbakova, P.V.3
  • 47
    • 78049441698 scopus 로고    scopus 로고
    • Separate roles of structured and unstructured regions of Y-family DNA polymerases
    • Ohmori, H., Hanafusa, T., Ohashi, E., and Vaziri, C. (2009) Separate roles of structured and unstructured regions of Y-family DNA polymerases. Adv. Protein Chem. Struct. Biol. 78, 99-146
    • (2009) Adv. Protein Chem. Struct. Biol. , vol.78 , pp. 99-146
    • Ohmori, H.1    Hanafusa, T.2    Ohashi, E.3    Vaziri, C.4
  • 48
    • 63249113718 scopus 로고    scopus 로고
    • Interaction with DNA polymerase ε is required for nuclear accumulation of REV1 and suppression of spontaneous mutations in human cells
    • Akagi, J., Masutani, C., Kataoka, Y., Kan, T., Ohashi, E., Mori, T., Ohmori, H., Hanaoka, F. (2009) Interaction with DNA polymerase ε is required for nuclear accumulation of REV1 and suppression of spontaneous mutations in human cells. DNA Repair 8, 585-599
    • (2009) DNA Repair , vol.8 , pp. 585-599
    • Akagi, J.1    Masutani, C.2    Kataoka, Y.3    Kan, T.4    Ohashi, E.5    Mori, T.6    Ohmori, H.7    Hanaoka, F.8


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