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Volumn 406, Issue 1, 2011, Pages 9-17

Crystal structure of SUMO-modified proliferating cell nuclear antigen

Author keywords

DNA recombination; DNA repair; DNA replication; protein DNA interactions; translesion synthesis

Indexed keywords

CYCLINE; DNA POLYMERASE; SUMO PROTEIN; UBIQUITIN;

EID: 79151484195     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.12.015     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S.R., Kong X.P., Gary S., Burgers P.M., and Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA Cell 79 1994 1233 1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.R.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 2
    • 0032102260 scopus 로고    scopus 로고
    • Clamping down on clamps and clamp loaders-the eukaryotic replication factor C
    • Mossi R., and Hubscher U. Clamping down on clamps and clamp loaders-the eukaryotic replication factor C Eur. J. Biochem. 254 1998 209 216
    • (1998) Eur. J. Biochem. , vol.254 , pp. 209-216
    • Mossi, R.1    Hubscher, U.2
  • 4
    • 0032031972 scopus 로고    scopus 로고
    • PCNA binding through a conserved motif
    • Warbrick E. PCNA binding through a conserved motif BioEssays 20 1998 195 199
    • (1998) BioEssays , vol.20 , pp. 195-199
    • Warbrick, E.1
  • 5
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick E. The puzzle of PCNA's many partners BioEssays 22 2000 997 1006
    • (2000) BioEssays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 7
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga G., and Hubscher U. Proliferating cell nuclear antigen (PCNA): a dancer with many partners J. Cell Sci. 116 2003 3051 3060
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 8
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan G.L., Pfander B., and Jentsch S. PCNA, the maestro of the replication fork Cell 129 2007 665 679
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 9
    • 0001298056 scopus 로고    scopus 로고
    • PCNA binding proteins
    • Tsurimoto T. PCNA binding proteins Front. Biosci. 4 1999 d849 858
    • (1999) Front. Biosci. , vol.4 , pp. 849-858
    • Tsurimoto, T.1
  • 10
    • 63049106529 scopus 로고    scopus 로고
    • Regulating post-translational modifications of the eukaryotic replication clamp PCNA
    • Ulrich H.D. Regulating post-translational modifications of the eukaryotic replication clamp PCNA DNA Repair 8 2009 461 469
    • (2009) DNA Repair , vol.8 , pp. 461-469
    • Ulrich, H.D.1
  • 11
    • 29244473887 scopus 로고    scopus 로고
    • SUMO keeps a check on recombination during DNA replication
    • Ulrich H.D., Vogel S., and Davies A.A. SUMO keeps a check on recombination during DNA replication Cell Cycle 4 2005 1699 1702
    • (2005) Cell Cycle , vol.4 , pp. 1699-1702
    • Ulrich, H.D.1    Vogel, S.2    Davies, A.A.3
  • 12
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich H.D., and Walden H. Ubiquitin signalling in DNA replication and repair Nat. Rev., Mol. Cell Biol. 11 2010 479 489
    • (2010) Nat. Rev., Mol. Cell Biol. , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 13
    • 32644454570 scopus 로고    scopus 로고
    • Sumoylation of PCNA: Wrestling with recombination at stalled replication forks
    • Watts F.Z. Sumoylation of PCNA: wrestling with recombination at stalled replication forks DNA Repair 5 2006 399 403
    • (2006) DNA Repair , vol.5 , pp. 399-403
    • Watts, F.Z.1
  • 14
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • Bergink S., and Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair Nature 458 2009 461 467
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 15
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P., and Ulrich H.D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation Nature 425 2003 188 191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 16
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO Nature 419 2002 135 141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 17
    • 29144499065 scopus 로고    scopus 로고
    • Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis
    • Bienko M., Green C.M., Crosetto N., Rudolf F., Zapart G., and Coull B. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis Science 310 2005 1821 1824
    • (2005) Science , vol.310 , pp. 1821-1824
    • Bienko, M.1    Green, C.M.2    Crosetto, N.3    Rudolf, F.4    Zapart, G.5    Coull, B.6
  • 18
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche P.L., Wing J., and Lehmann A.R. Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage Mol. Cell 14 2004 491 500
    • (2004) Mol. Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 19
    • 0032510731 scopus 로고    scopus 로고
    • MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway
    • Broomfield S., Chow B.L., and Xiao W. MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway Proc. Natl Acad. Sci. USA 95 1998 5678 5683
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5678-5683
    • Broomfield, S.1    Chow, B.L.2    Xiao, W.3
  • 20
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., and Pickart C.M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair Cell 96 1999 645 653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 21
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin- conjugating enzymes in DNA repair
    • Ulrich H.D., and Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair EMBO J. 19 2000 3388 3397
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 22
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B., Moldovan G.L., Sacher M., Hoege C., and Jentsch S. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase Nature 436 2005 428 433
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 23
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E., Chen S.H., Davies A.A., Huttner D., Krejci L., Sung P., and Ulrich H.D. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p Mol. Cell 19 2005 123 133
    • (2005) Mol. Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.H.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 24
    • 2542453681 scopus 로고    scopus 로고
    • Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein
    • Krejci L., Macris M., Li Y., Van Komen S., Villemain J., and Ellenberger T. Role of ATP hydrolysis in the antirecombinase function of Saccharomyces cerevisiae Srs2 protein J. Biol. Chem. 279 2004 23193 23199
    • (2004) J. Biol. Chem. , vol.279 , pp. 23193-23199
    • Krejci, L.1    MacRis, M.2    Li, Y.3    Van Komen, S.4    Villemain, J.5    Ellenberger, T.6
  • 25
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute X., Jeusset J., Soustelle C., Kowalczykowski S.C., Le Cam E., and Fabre F. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments Nature 423 2003 309 312
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 26
    • 77949875253 scopus 로고    scopus 로고
    • Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis
    • Chen J.J., Ai Y.X., Wang J.L., Haracska L., and Zhuang Z.H. Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis Nat. Chem. Biol. 6 2010 270 272
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 270-272
    • Chen, J.J.1    Ai, Y.X.2    Wang, J.L.3    Haracska, L.4    Zhuang, Z.H.5
  • 27
    • 70350417485 scopus 로고    scopus 로고
    • Synthesis of free and proliferating cell nuclear antigen-bound polyubiquitin chains by the RING E3 ubiquitin ligase Rad5
    • Carlile C.M., Pickart C.M., Matunis M.J., and Cohen R.E. Synthesis of free and proliferating cell nuclear antigen-bound polyubiquitin chains by the RING E3 ubiquitin ligase Rad5 J. Biol. Chem. 284 2009 29326 29334
    • (2009) J. Biol. Chem. , vol.284 , pp. 29326-29334
    • Carlile, C.M.1    Pickart, C.M.2    Matunis, M.J.3    Cohen, R.E.4
  • 28
    • 77950517365 scopus 로고    scopus 로고
    • Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange
    • Freudenthal B.D., Gakhar L., Ramaswamy S., and Washington M.T. Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange Nat. Struct. Mol. Biol. 17 2010 479 484
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 479-484
    • Freudenthal, B.D.1    Gakhar, L.2    Ramaswamy, S.3    Washington, M.T.4
  • 29
    • 57649128297 scopus 로고    scopus 로고
    • Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis
    • Freudenthal B.D., Ramaswamy S., Hingorani M.M., and Washington M.T. Structure of a mutant form of proliferating cell nuclear antigen that blocks translesion DNA synthesis Biochemistry 47 2008 13354 13361
    • (2008) Biochemistry , vol.47 , pp. 13354-13361
    • Freudenthal, B.D.1    Ramaswamy, S.2    Hingorani, M.M.3    Washington, M.T.4
  • 30
    • 77956026751 scopus 로고    scopus 로고
    • Pre-steady state kinetic studies of the fidelity of nucleotide incorporation by yeast DNA polymerase delta
    • Dieckman L.M., Johnson R.E., Prakash S., and Washington M.T. Pre-steady state kinetic studies of the fidelity of nucleotide incorporation by yeast DNA polymerase delta Biochemistry 49 2010 7344 7350
    • (2010) Biochemistry , vol.49 , pp. 7344-7350
    • Dieckman, L.M.1    Johnson, R.E.2    Prakash, S.3    Washington, M.T.4
  • 31
    • 21244448890 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen promotes translesion synthesis by DNA polymerase zeta
    • Garg P., Stith C.M., Majka J., and Burgers P.M.J. Proliferating cell nuclear antigen promotes translesion synthesis by DNA polymerase zeta J. Biol. Chem. 280 2005 23446 23450
    • (2005) J. Biol. Chem. , vol.280 , pp. 23446-23450
    • Garg, P.1    Stith, C.M.2    Majka, J.3    Burgers, P.M.J.4
  • 33
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read R.J. Pushing the boundaries of molecular replacement with maximum likelihood Acta Crystallogr., Sect. D: Biol. Crystallogr. 57 2001 1373 1382
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 38
    • 69749124557 scopus 로고    scopus 로고
    • Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA
    • Yunus A.A., and Lima C.D. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA Mol. Cell 35 2009 669 682
    • (2009) Mol. Cell , vol.35 , pp. 669-682
    • Yunus, A.A.1    Lima, C.D.2
  • 39
    • 33747854122 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae rev6-1 mutation, which inhibits both the lesion bypass and the recombination mode of DNA damage tolerance, is an allele of POL30, encoding proliferating cell nuclear antigen
    • Zhang H.S., Gibbs P.E.M., and Lawrence C.W. The Saccharomyces cerevisiae rev6-1 mutation, which inhibits both the lesion bypass and the recombination mode of DNA damage tolerance, is an allele of POL30, encoding proliferating cell nuclear antigen Genetics 173 2006 1983 1989
    • (2006) Genetics , vol.173 , pp. 1983-1989
    • Zhang, H.S.1    Gibbs, P.E.M.2    Lawrence, C.W.3
  • 40
    • 24944543952 scopus 로고    scopus 로고
    • A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously
    • Indiani C., McInerney P., Georgescu R., Goodman M.F., and O'Donnell M. A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously Mol. Cell 19 2005 805 815
    • (2005) Mol. Cell , vol.19 , pp. 805-815
    • Indiani, C.1    McInerney, P.2    Georgescu, R.3    Goodman, M.F.4    O'Donnell, M.5
  • 41
    • 77949567581 scopus 로고    scopus 로고
    • Coordinating DNA polymerase traffic during high and low fidelity synthesis
    • Sutton M.D. Coordinating DNA polymerase traffic during high and low fidelity synthesis Biochim. Biophys. Acta 1804 2010 1167 1179
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1167-1179
    • Sutton, M.D.1
  • 42
    • 77949570096 scopus 로고    scopus 로고
    • Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis
    • Zhuang Z.H., and Ai Y.X. Processivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesis Biochim. Biophys. Acta 1804 2010 1081 1093
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1081-1093
    • Zhuang, Z.H.1    Ai, Y.X.2


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