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Volumn 29, Issue 15, 2010, Pages 2611-2622

Elg1, an alternative subunit of the RFC clamp loader, preferentially interacts with SUMOylated PCNA

Author keywords

genome stability; PCNA modification; postreplicational repair

Indexed keywords

HELICASE; PROTEIN DERIVATIVE; PROTEIN ELG1; REPLICATION FACTOR C; SUMO PROTEIN; UNCLASSIFIED DRUG;

EID: 77955416458     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2010.128     Document Type: Article
Times cited : (91)

References (60)
  • 3
    • 13844320317 scopus 로고    scopus 로고
    • The Elg1 replication factor C-like complex: A novel guardian of genome stability
    • Aroya SB, Kupiec M (2005) The Elg1 replication factor C-like complex: a novel guardian of genome stability. DNA Repair (Amst) 4: 409-417
    • (2005) DNA Repair (Amst) , vol.4 , pp. 409-417
    • Aroya, S.B.1    Kupiec, M.2
  • 4
    • 11144261727 scopus 로고    scopus 로고
    • Increased genome instability and telomere length in the elg1-deficient Saccharomyces cerevisiae mutant are regulated by S-phase checkpoints
    • Banerjee S, Myung K (2004) Increased genome instability and telomere length in the elg1-deficient Saccharomyces cerevisiae mutant are regulated by S-phase checkpoints. Eukaryot Cell 3: 1557-1566
    • (2004) Eukaryot Cell , vol.3 , pp. 1557-1566
    • Banerjee, S.1    Myung, K.2
  • 5
    • 0041966011 scopus 로고    scopus 로고
    • Elg1 forms an alternative RFC complex important for DNA replication and genome integrity
    • Bellaoui M, Chang M, Ou J, Xu H, Boone C, Brown GW (2003) Elg1 forms an alternative RFC complex important for DNA replication and genome integrity. EMBO J 22: 4304-4313
    • (2003) EMBO J , vol.22 , pp. 4304-4313
    • Bellaoui, M.1    Chang, M.2    Ou, J.3    Xu, H.4    Boone, C.5    Brown, G.W.6
  • 6
    • 0042191693 scopus 로고    scopus 로고
    • ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C
    • Ben-Aroya S, Koren A, Liefshitz B, Steinlauf R, Kupiec M (2003) ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C. Proc Natl Acad Sci USA 100: 9906-9911
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9906-9911
    • Ben-Aroya, S.1    Koren, A.2    Liefshitz, B.3    Steinlauf, R.4    Kupiec, M.5
  • 8
    • 35148847451 scopus 로고    scopus 로고
    • Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression
    • Blastyak A, Pinter L, Unk I, Prakash L, Prakash S, Haracska L (2007) Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression. Mol Cell 28: 167-175
    • (2007) Mol Cell , vol.28 , pp. 167-175
    • Blastyak, A.1    Pinter, L.2    Unk, I.3    Prakash, L.4    Prakash, S.5    Haracska, L.6
  • 9
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman GD, O0Donnell M, Kuriyan J (2004) Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429: 724-730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 10
    • 57749169348 scopus 로고    scopus 로고
    • SUMOylation regulates Rad18-mediated template switch
    • Branzei D, Vanoli F, Foiani M (2008) SUMOylation regulates Rad18-mediated template switch. Nature 456: 915-920
    • (2008) Nature , vol.456 , pp. 915-920
    • Branzei, D.1    Vanoli, F.2    Foiani, M.3
  • 11
    • 33745203951 scopus 로고    scopus 로고
    • Overproduction and purification of RFC-related clamp loaders and PCNA-related clamps from Saccharomyces cerevisiae
    • Bylund GO, Majka J, Burgers PM (2006) Overproduction and purification of RFC-related clamp loaders and PCNA-related clamps from Saccharomyces cerevisiae. Methods Enzymol 409: 1-11
    • (2006) Methods Enzymol , vol.409 , pp. 1-11
    • Bylund, G.O.1    Majka, J.2    Burgers, P.M.3
  • 12
    • 27144448514 scopus 로고    scopus 로고
    • The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner
    • Chen S, Davies AA, Sagan D, Ulrich HD (2005) The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner. Nucleic Acids Res 33: 5878-5886
    • (2005) Nucleic Acids Res , vol.33 , pp. 5878-5886
    • Chen, S.1    Davies, A.A.2    Sagan, D.3    Ulrich, H.D.4
  • 13
    • 36248991353 scopus 로고    scopus 로고
    • The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA
    • Chilkova O, Stenlund P, Isoz I, Stith CM, Grabowski P, Lundstrom EB, Burgers PM, Johansson E (2007) The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA. Nucleic Acids Res 35: 6588-6597
    • (2007) Nucleic Acids Res , vol.35 , pp. 6588-6597
    • Chilkova, O.1    Stenlund, P.2    Isoz, I.3    Stith, C.M.4    Grabowski, P.5    Lundstrom, E.B.6    Burgers, P.M.7    Johansson, E.8
  • 14
    • 46649089698 scopus 로고    scopus 로고
    • The N-and C-termini of Elg1 contribute to the maintenance of genome stability
    • Davidson MB, Brown GW (2008) The N-and C-termini of Elg1 contribute to the maintenance of genome stability. DNA Repair (Amst) 7: 1221-1232
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1221-1232
    • Davidson, M.B.1    Brown, G.W.2
  • 15
    • 0344994570 scopus 로고    scopus 로고
    • Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus
    • De Felice M, Sensen CW, Charlebois RL, Rossi M, Pisani FM (1999) Two DNA polymerase sliding clamps from the thermophilic archaeon Sulfolobus solfataricus. J Mol Biol 291: 47-57
    • (1999) J Mol Biol , vol.291 , pp. 47-57
    • De Felice, M.1    Sensen, C.W.2    Charlebois, R.L.3    Rossi, M.4    Pisani, F.M.5
  • 16
    • 0030857979 scopus 로고    scopus 로고
    • Mutations in yeast proliferating cell nuclear antigen define distinct sites for interaction with DNA polymerase delta and DNA polymerase epsilon
    • Eissenberg JC, Ayyagari R, Gomes XV, Burgers PM (1997) Mutations in yeast proliferating cell nuclear antigen define distinct sites for interaction with DNA polymerase delta and DNA polymerase epsilon. Mol Cell Biol 17: 6367-6378
    • (1997) Mol Cell Biol , vol.17 , pp. 6367-6378
    • Eissenberg, J.C.1    Ayyagari, R.2    Gomes, X.V.3    Burgers, P.M.4
  • 17
    • 0026543506 scopus 로고
    • Identification of replication factor C from Saccharomyces cerevisiae: A component of the leading-strand DNA replication complex
    • Fien K, Stillman B (1992) Identification of replication factor C from Saccharomyces cerevisiae: a component of the leading-strand DNA replication complex. Mol Cell Biol 12: 155-163
    • (1992) Mol Cell Biol , vol.12 , pp. 155-163
    • Fien, K.1    Stillman, B.2
  • 18
    • 33749617398 scopus 로고    scopus 로고
    • Mms2-Ubc13-dependent and-independent roles of Rad5 ubiquitin ligase in postreplication repair and translesion DNA synthesis in Saccharomyces cerevisiae
    • Gangavarapu V, Haracska L, Unk I, Johnson RE, Prakash S, Prakash L (2006) Mms2-Ubc13-dependent and-independent roles of Rad5 ubiquitin ligase in postreplication repair and translesion DNA synthesis in Saccharomyces cerevisiae. Mol Cell Biol 26: 7783-7790
    • (2006) Mol Cell Biol , vol.26 , pp. 7783-7790
    • Gangavarapu, V.1    Haracska, L.2    Unk, I.3    Johnson, R.E.4    Prakash, S.5    Prakash, L.6
  • 19
    • 0035051062 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae CTF18 and CTF4 are required for sister chromatid cohesion
    • Hanna JS, Kroll ES, Lundblad V, Spencer FA (2001) Saccharomyces cerevisiae CTF18 and CTF4 are required for sister chromatid cohesion. Mol Cell Biol 21: 3144-3158
    • (2001) Mol Cell Biol , vol.21 , pp. 3144-3158
    • Hanna, J.S.1    Kroll, E.S.2    Lundblad, V.3    Spencer, F.A.4
  • 20
    • 33745845186 scopus 로고    scopus 로고
    • Functional and physical interaction of yeast Mgs1 with PCNA: Impact on RAD6-dependent DNA damage tolerance
    • Hishida T, Ohya T, Kubota Y, Kamada Y, Shinagawa H (2006) Functional and physical interaction of yeast Mgs1 with PCNA: impact on RAD6-dependent DNA damage tolerance. Mol Cell Biol 26: 5509-5517
    • (2006) Mol Cell Biol , vol.26 , pp. 5509-5517
    • Hishida, T.1    Ohya, T.2    Kubota, Y.3    Kamada, Y.4    Shinagawa, H.5
  • 21
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419: 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
  • 22
    • 0141482059 scopus 로고    scopus 로고
    • A genomewide screen in Saccharomyces cerevisiae for genes that suppress the accumulation of mutations
    • Huang ME, Rio AG, Nicolas A, Kolodner RD (2003) A genomewide screen in Saccharomyces cerevisiae for genes that suppress the accumulation of mutations. Proc Natl Acad Sci USA 100: 11529-11534
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11529-11534
    • Huang, M.E.1    Rio, A.G.2    Nicolas, A.3    Kolodner, R.D.4
  • 24
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James P, Halladay J, Craig EA (1996) Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144: 1425-1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 25
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • DOI 10.1016/S0092-8674(01)00463-9
    • Jeruzalmi D, O0Donnell M, Kuriyan J (2001) Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106: 429-441 (Pubitemid 32786987)
    • (2001) Cell , vol.106 , Issue.4 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 26
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson ES, Gupta AA (2001) An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106: 735-744
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 27
    • 0141504148 scopus 로고    scopus 로고
    • Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability
    • Kanellis P, Agyei R, Durocher D (2003) Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability. Curr Biol 13: 1583-1595
    • (2003) Curr Biol , vol.13 , pp. 1583-1595
    • Kanellis, P.1    Agyei, R.2    Durocher, D.3
  • 28
    • 0029163487 scopus 로고
    • Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps
    • Kelman Z, O'Donnell M (1995) Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps. Nucleic Acids Res 23: 3613-3620
    • (1995) Nucleic Acids Res , vol.23 , pp. 3613-3620
    • Kelman, Z.1    O'Donnell, M.2
  • 29
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O (2007) SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep 8: 550-555
    • (2007) EMBO Rep , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 30
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79: 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
  • 31
    • 50849103297 scopus 로고    scopus 로고
    • Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA
    • Le Breton C, Dupaigne P, Robert T, Le Cam E, Gangloff S, Fabre F, Veaute X (2008) Srs2 removes deadly recombination intermediates independently of its interaction with SUMO-modified PCNA. Nucleic Acids Res 36: 4964-4974
    • (2008) Nucleic Acids Res , vol.36 , pp. 4964-4974
    • Le Breton, C.1    Dupaigne, P.2    Robert, T.3    Le Cam, E.4    Gangloff, S.5    Fabre, F.6    Veaute, X.7
  • 32
    • 29144501653 scopus 로고    scopus 로고
    • Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts
    • Leach CA, Michael WM (2005) Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts. J Cell Biol 171: 947-954
    • (2005) J Cell Biol , vol.171 , pp. 947-954
    • Leach, C.A.1    Michael, W.M.2
  • 34
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka J, Burgers PM (2004) The PCNA-RFC families of DNA clamps and clamp loaders. Prog Nucleic Acid Res Mol Biol 78: 227-260
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 35
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty A, Dumont X, Kaghad M, Caput D (2000) Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem 275: 36316-36323
    • (2000) J Biol Chem , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 36
    • 33747882922 scopus 로고    scopus 로고
    • PCNA controls establishment of sister chromatid cohesion during S phase
    • Moldovan GL, Pfander B, Jentsch S (2006) PCNA controls establishment of sister chromatid cohesion during S phase. Mol Cell 23: 723-732
    • (2006) Mol Cell , vol.23 , pp. 723-732
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 37
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan GL, Pfander B, Jentsch S (2007) PCNA, the maestro of the replication fork. Cell 129: 665-679
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 39
    • 33846929135 scopus 로고    scopus 로고
    • Role of Elg1 protein in double strand break repair
    • Ogiwara H, Ui A, Enomoto T, Seki M (2007) Role of Elg1 protein in double strand break repair. Nucleic Acids Res 35: 353-362
    • (2007) Nucleic Acids Res , vol.35 , pp. 353-362
    • Ogiwara, H.1    Ui, A.2    Enomoto, T.3    Seki, M.4
  • 40
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E, Chen S, Davies AA, Huttner D, Krejci L, Sung P, Ulrich HD (2005) Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 19: 123-133
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 41
    • 33847381960 scopus 로고    scopus 로고
    • Contributions of ubiquitin-and PCNA-binding domains to the activity of Polymerase eta in Saccharomyces cerevisiae
    • Parker JL, Bielen AB, Dikic I, Ulrich HD (2007) Contributions of ubiquitin-and PCNA-binding domains to the activity of Polymerase eta in Saccharomyces cerevisiae. Nucleic Acids Res 35: 881-889
    • (2007) Nucleic Acids Res , vol.35 , pp. 881-889
    • Parker, J.L.1    Bielen, A.B.2    Dikic, I.3    Ulrich, H.D.4
  • 43
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S (2005) SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436: 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
  • 44
    • 0035692614 scopus 로고    scopus 로고
    • Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance
    • Scholes DT, Banerjee M, Bowen B, Curcio MJ (2001) Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance. Genetics 159: 1449-1465
    • (2001) Genetics , vol.159 , pp. 1449-1465
    • Scholes, D.T.1    Banerjee, M.2    Bowen, B.3    Curcio, M.J.4
  • 46
    • 2942695713 scopus 로고    scopus 로고
    • Mutator genes for suppression of gross chromosomal rearrangements identified by a genome-wide screening in Saccharomyces cerevisiae
    • Smith S, Hwang JY, Banerjee S, Majeed A, Gupta A, Myung K (2004) Mutator genes for suppression of gross chromosomal rearrangements identified by a genome-wide screening in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 101: 9039-9044
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9039-9044
    • Smith, S.1    Hwang, J.Y.2    Banerjee, S.3    Majeed, A.4    Gupta, A.5    Myung, K.6
  • 47
    • 1242297066 scopus 로고    scopus 로고
    • ELG1, a regulator of genome stability, has a role in telomere length regulation and in silencing
    • Smolikov S, Mazor Y, Krauskopf A (2004) ELG1, a regulator of genome stability, has a role in telomere length regulation and in silencing. Proc Natl Acad Sci USA 101: 1656-1661
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1656-1661
    • Smolikov, S.1    Mazor, Y.2    Krauskopf, A.3
  • 49
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damageinduced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter P, Ulrich HD (2003) Control of spontaneous and damageinduced mutagenesis by SUMO and ubiquitin conjugation. Nature 425: 188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 51
    • 0024509284 scopus 로고
    • Purification of a cellular replication factor, RF-C, that is required for coordinated synthesis of leading and lagging strands during simian virus 40 DNA replication in vitro
    • Tsurimoto T, Stillman B (1989) Purification of a cellular replication factor, RF-C, that is required for coordinated synthesis of leading and lagging strands during simian virus 40 DNA replication in vitro. Mol Cell Biol 9: 609-619
    • (1989) Mol Cell Biol , vol.9 , pp. 609-619
    • Tsurimoto, T.1    Stillman, B.2
  • 52
    • 0026089096 scopus 로고
    • Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins
    • Tsurimoto T, Stillman B (1991) Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins. J Biol Chem 266: 1950-1960
    • (1991) J Biol Chem , vol.266 , pp. 1950-1960
    • Tsurimoto, T.1    Stillman, B.2
  • 53
    • 63049106529 scopus 로고    scopus 로고
    • Regulating post-translational modifications of the eukaryotic replication clamp PCNA
    • Ulrich HD (2009) Regulating post-translational modifications of the eukaryotic replication clamp PCNA. DNA Repair (Amst) 8: q461-469
    • (2009) DNA Repair (Amst) , vol.8
    • Ulrich, H.D.1
  • 55
    • 0032031972 scopus 로고    scopus 로고
    • PCNA binding through a conserved motif
    • Warbrick E (1998) PCNA binding through a conserved motif. Bioessays 20: 195-199
    • (1998) Bioessays , vol.20 , pp. 195-199
    • Warbrick, E.1
  • 56
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick E (2000) The puzzle of PCNA's many partners. Bioessays 22: 997-1006
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 57
    • 38049079191 scopus 로고    scopus 로고
    • Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae
    • Windecker H, Ulrich HD (2008) Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae. J Mol Biol 376: 221-231
    • (2008) J Mol Biol , vol.376 , pp. 221-231
    • Windecker, H.1    Ulrich, H.D.2
  • 58
    • 0035836496 scopus 로고    scopus 로고
    • A novel PCNA-binding motif identified by the panning of a random peptide display library
    • Xu H, Zhang P, Liu L, Lee MY (2001) A novel PCNA-binding motif identified by the panning of a random peptide display library. Biochemistry 40: 4512-4520
    • (2001) Biochemistry , vol.40 , pp. 4512-4520
    • Xu, H.1    Zhang, P.2    Liu, L.3    Lee, M.Y.4
  • 59
    • 69749124557 scopus 로고    scopus 로고
    • Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA
    • Yunus AA, Lima CD (2009) Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol Cell 35: 669-682
    • (2009) Mol Cell , vol.35 , pp. 669-682
    • Yunus, A.A.1    Lima, C.D.2
  • 60
    • 44449138846 scopus 로고    scopus 로고
    • Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme
    • Zhuang Z, Johnson RE, Haracska L, Prakash L, Prakash S, Benkovic SJ (2008) Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme. Proc Natl Acad Sci USA 105: 5361-5366
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5361-5366
    • Zhuang, Z.1    Johnson, R.E.2    Haracska, L.3    Prakash, L.4    Prakash, S.5    Benkovic, S.J.6


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