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Volumn 23, Issue 4, 2015, Pages 724-733

Structurally distinct ubiquitin- and sumo-modified PCNA: Implications for their distinct roles in the DNA damage response

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN; SUMO 1 PROTEIN;

EID: 84930188600     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.02.008     Document Type: Article
Times cited : (38)

References (63)
  • 1
    • 84857748099 scopus 로고    scopus 로고
    • Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2
    • A.A. Armstrong, F. Mohideen, and C.D. Lima Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2 Nature 483 2012 59 63
    • (2012) Nature , vol.483 , pp. 59-63
    • Armstrong, A.A.1    Mohideen, F.2    Lima, C.D.3
  • 2
    • 0029001791 scopus 로고
    • A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair
    • R. Ayyagari, K.J. Impellizzeri, B.L. Yoder, S.L. Gary, and P.M. Burgers A mutational analysis of the yeast proliferating cell nuclear antigen indicates distinct roles in DNA replication and DNA repair Mol. Cell. Biol. 15 1995 4420 4429
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4420-4429
    • Ayyagari, R.1    Impellizzeri, K.J.2    Yoder, B.L.3    Gary, S.L.4    Burgers, P.M.5
  • 8
    • 77949875253 scopus 로고    scopus 로고
    • Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis
    • J.J. Chen, Y.X. Ai, J.L. Wang, L. Haracska, and Z.H. Zhuang 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
  • 9
    • 77958554597 scopus 로고    scopus 로고
    • Software for the high-throughput collection of SAXS data using an enhanced Blu-Ice/DCS control system
    • S. Classen, I. Rodic, J. Holton, G.L. Hura, M. Hammel, and J.A. Tainer Software for the high-throughput collection of SAXS data using an enhanced Blu-Ice/DCS control system J. Synchrotron Radiat. 17 2010 774 781
    • (2010) J. Synchrotron Radiat. , vol.17 , pp. 774-781
    • Classen, S.1    Rodic, I.2    Holton, J.3    Hura, G.L.4    Hammel, M.5    Tainer, J.A.6
  • 14
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Y. Duan, C. Wu, S. Chowdhury, M.C. Lee, G.M. Xiong, W. Zhang, R. Yang, P. Cieplak, R. Luo, and T. Lee A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations J. Comput. Chem. 24 2003 1999 2012
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.M.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10
  • 17
    • 77950517365 scopus 로고    scopus 로고
    • Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange
    • B.D. Freudenthal, L. Gakhar, S. Ramaswamy, and M.T. Washington 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
  • 19
    • 84867508210 scopus 로고    scopus 로고
    • Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS)
    • M. Hammel Validation of macromolecular flexibility in solution by small-angle X-ray scattering (SAXS) Eur. Biophys. J. 41 2012 789 799
    • (2012) Eur. Biophys. J. , vol.41 , pp. 789-799
    • Hammel, M.1
  • 20
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • L. Hicke Protein regulation by monoubiquitin Nat. Rev. Mol. Cell Biol. 2 2001 195 201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 21
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • C. Hoege, B. Pfander, G.L. Moldovan, G. Pyrowolakis, and S. Jentsch 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
  • 23
    • 33845625617 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen loaded onto double-stranded DNA: Dynamics, minor groove interactions and functional implications
    • I. Ivanov, B.R. Chapados, J.A. McCammon, and J.A. Tainer Proliferating cell nuclear antigen loaded onto double-stranded DNA: dynamics, minor groove interactions and functional implications Nucleic Acids Res. 34 2006 6023 6033
    • (2006) Nucleic Acids Res. , vol.34 , pp. 6023-6033
    • Ivanov, I.1    Chapados, B.R.2    McCammon, J.A.3    Tainer, J.A.4
  • 24
    • 0039118382 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen: More than a clamp for DNA polymerases
    • Z.O. Jonsson, and U. Hubscher Proliferating cell nuclear antigen: more than a clamp for DNA polymerases Bioessays 19 1997 967 975
    • (1997) Bioessays , vol.19 , pp. 967-975
    • Jonsson, Z.O.1    Hubscher, U.2
  • 27
    • 0031045565 scopus 로고    scopus 로고
    • PCNA: Structure, functions and interactions
    • Z. Kelman PCNA: structure, functions and interactions Oncogene 14 1997 629 640
    • (1997) Oncogene , vol.14 , pp. 629-640
    • Kelman, Z.1
  • 29
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • T.S. Krishna, X.P. Kong, S. Gary, P.M. Burgers, and J. Kuriyan 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.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 30
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • B. Kuhlman, and D. Baker Native protein sequences are close to optimal for their structures Proc. Natl. Acad. Sci. USA 97 2000 10383 10388
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 32
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • G. Maga, and U. Hubscher 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
  • 33
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • G.L. Moldovan, B. Pfander, and S. Jentsch 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
  • 35
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • E. Papouli, S.H. Chen, A.A. Davies, D. Huttner, L. Krejci, P. Sung, and H.D. Ulrich 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
  • 36
    • 84871206469 scopus 로고    scopus 로고
    • A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA
    • J.L. Parker, and H.D. Ulrich A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA Nucleic Acids Res. 40 2012 11380 11388
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11380-11388
    • Parker, J.L.1    Ulrich, H.D.2
  • 37
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • M. Pelikan, G.L. Hura, and M. Hammel Structure and flexibility within proteins as identified through small angle X-ray scattering Gen. Physiol. Biophys. 28 2009 174 189
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 39
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • B. Pfander, G.L. Moldovan, M. Sacher, C. Hoege, and S. Jentsch 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
  • 42
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • C.D. Putnam, M. Hammel, G.L. Hura, and J.A. Tainer X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution Q. Rev. Biophys. 40 2007 191 285
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 43
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • R.P. Rambo, and J.A. Tainer Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering Curr. Opin. Struct. Biol. 20 2010 128 137
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 44
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • R.P. Rambo, and J.A. Tainer Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law Biopolymers 95 2011 559 571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 45
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • R.P. Rambo, and J.A. Tainer Accurate assessment of mass, models and resolution by small-angle scattering Nature 496 2013 477 481
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 46
    • 84925454486 scopus 로고    scopus 로고
    • Methods for using new conceptual tools and parameters to assess RNA structure by small-angle X-ray scattering
    • F.E. Reyes, C.R. Schwartz, J.A. Tainer, and R.P. Rambo Methods for using new conceptual tools and parameters to assess RNA structure by small-angle X-ray scattering Methods Enzymol. 549 2014 235 263
    • (2014) Methods Enzymol. , vol.549 , pp. 235-263
    • Reyes, F.E.1    Schwartz, C.R.2    Tainer, J.A.3    Rambo, R.P.4
  • 48
    • 79953296212 scopus 로고    scopus 로고
    • Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate
    • A. Saha, S. Lewis, G. Kleiger, B. Kuhlman, and R.J. Deshaies Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate Mol. Cell 42 2011 75 83
    • (2011) Mol. Cell , vol.42 , pp. 75-83
    • Saha, A.1    Lewis, S.2    Kleiger, G.3    Kuhlman, B.4    Deshaies, R.J.5
  • 49
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • D. Schneidman-Duhovny, M. Hammel, and A. Sali FoXS: a web server for rapid computation and fitting of SAXS profiles Nucleic Acids Res. 38 2010 W540 W544
    • (2010) Nucleic Acids Res. , vol.38 , pp. W540-W544
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 50
    • 84882940564 scopus 로고    scopus 로고
    • Accurate SAXS profile computation and its assessment by contrast variation experiments
    • D. Schneidman-Duhovny, M. Hammel, J.A. Tainer, and A. Sali Accurate SAXS profile computation and its assessment by contrast variation experiments Biophys. J. 105 2013 962 974
    • (2013) Biophys. J. , vol.105 , pp. 962-974
    • Schneidman-Duhovny, D.1    Hammel, M.2    Tainer, J.A.3    Sali, A.4
  • 51
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • R. Steinacher, and P. Schar Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation Curr. Biol. 15 2005 616 623
    • (2005) Curr. Biol. , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 52
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • P. Stelter, and H.D. Ulrich 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
  • 55
    • 33646650705 scopus 로고
    • Reversible multiple time scale molecular-dynamics
    • M. Tuckerman, B.J. Berne, and G.J. Martyna Reversible multiple time scale molecular-dynamics J. Chem. Phys. 97 1992 1990 2001
    • (1992) J. Chem. Phys. , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyna, G.J.3
  • 56
    • 25844437172 scopus 로고    scopus 로고
    • Mutual interactions between the SUMO and ubiquitin systems: A plea of no contest
    • H.D. Ulrich Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest Trends Cell Biol. 15 2005 525 532
    • (2005) Trends Cell Biol. , vol.15 , pp. 525-532
    • Ulrich, H.D.1
  • 57
    • 84858147489 scopus 로고    scopus 로고
    • Ubiquitin and SUMO in DNA repair at a glance
    • H.D. Ulrich Ubiquitin and SUMO in DNA repair at a glance J. Cell Sci. 125 2012 249 254
    • (2012) J. Cell Sci. , vol.125 , pp. 249-254
    • Ulrich, H.D.1
  • 58
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • H.D. Ulrich, and H. Walden 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
  • 59
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • X. Veaute, J. Jeusset, C. Soustelle, S.C. Kowalczykowski, E. Le Cam, and F. Fabre 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
  • 60
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • S. Vijay-Kumar, C.E. Bugg, and W.J. Cook Structure of ubiquitin refined at 1.8 A resolution J. Mol. Biol. 194 1987 531 544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 61
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • G. Xu, J.S. Paige, and S.R. Jaffrey Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling Nat. Biotechnol. 28 2010 868 873
    • (2010) Nat. Biotechnol. , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 62
    • 84877725149 scopus 로고    scopus 로고
    • Regulatory role of ubiquitin in eukaryotic DNA translesion synthesis
    • K. Yang, C.P. Weinacht, and Z. Zhuang Regulatory role of ubiquitin in eukaryotic DNA translesion synthesis Biochemistry 52 2013 3217 3228
    • (2013) Biochemistry , vol.52 , pp. 3217-3228
    • Yang, K.1    Weinacht, C.P.2    Zhuang, Z.3
  • 63
    • 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
    • H. Zhang, P.E. Gibbs, and C.W. Lawrence 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.1    Gibbs, P.E.2    Lawrence, C.W.3


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