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Volumn 23, Issue 7, 2013, Pages 543-552

Dpb2 Integrates the Leading-Strand DNA Polymerase into the Eukaryotic Replisome

Author keywords

[No Author keywords available]

Indexed keywords

ANAZOLENE SODIUM; CDC45 PROTEIN, S CEREVISIAE; CELL CYCLE PROTEIN; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE ALPHA; DPB2 PROTEIN, S CEREVISIAE; FUCHSINE; HELICASE; MRC1 PROTEIN, S CEREVISIAE; MULTIPROTEIN COMPLEX; NUCLEAR PROTEIN; PRP8 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN;

EID: 84876108565     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2013.02.011     Document Type: Article
Times cited : (115)

References (48)
  • 1
    • 84875553632 scopus 로고    scopus 로고
    • New insights into replisome fluidity during chromosome replication
    • 10.1016/j.tibs.2012.10.003 Published online November 12, 2012
    • I. Kurth, and M. O'Donnell New insights into replisome fluidity during chromosome replication Trends Biochem. Sci. 2012 10.1016/j.tibs.2012.10.003 Published online November 12, 2012
    • (2012) Trends Biochem. Sci.
    • Kurth, I.1    O'Donnell, M.2
  • 2
    • 77951537332 scopus 로고    scopus 로고
    • Stoichiometry and architecture of active DNA replication machinery in Escherichia coli
    • R. Reyes-Lamothe, D.J. Sherratt, and M.C. Leake Stoichiometry and architecture of active DNA replication machinery in Escherichia coli Science 328 2010 498 501
    • (2010) Science , vol.328 , pp. 498-501
    • Reyes-Lamothe, R.1    Sherratt, D.J.2    Leake, M.C.3
  • 3
    • 84855453503 scopus 로고    scopus 로고
    • Single-molecule studies reveal the function of a third polymerase in the replisome
    • R.E. Georgescu, I. Kurth, and M.E. O'Donnell Single-molecule studies reveal the function of a third polymerase in the replisome Nat. Struct. Mol. Biol. 19 2012 113 116
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 113-116
    • Georgescu, R.E.1    Kurth, I.2    O'Donnell, M.E.3
  • 6
  • 7
    • 30944452765 scopus 로고    scopus 로고
    • Evidence that errors made by DNA polymerase α are corrected by DNA polymerase δ
    • DOI 10.1016/j.cub.2005.12.002, PII S0960982205015277
    • Y.I. Pavlov, C. Frahm, S.A. Nick McElhinny, A. Niimi, M. Suzuki, and T.A. Kunkel Evidence that errors made by DNA polymerase alpha are corrected by DNA polymerase delta Curr. Biol. 16 2006 202 207 (Pubitemid 43117436)
    • (2006) Current Biology , vol.16 , Issue.2 , pp. 202-207
    • Pavlov, Y.I.1    Frahm, C.2    McElhinny, S.A.N.3    Niimi, A.4    Suzuki, M.5    Kunkel, T.A.6
  • 8
    • 34447336941 scopus 로고    scopus 로고
    • Yeast DNA polymerase ε participates in leading-strand DNA replication
    • DOI 10.1126/science.1144067
    • Z.F. Pursell, I. Isoz, E.B. Lundström, E. Johansson, and T.A. Kunkel Yeast DNA polymerase epsilon participates in leading-strand DNA replication Science 317 2007 127 130 (Pubitemid 47056472)
    • (2007) Science , vol.317 , Issue.5834 , pp. 127-130
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.-B.3    Johansson, E.4    Kunkel, T.A.5
  • 9
    • 77953710831 scopus 로고    scopus 로고
    • SnapShot: The replisome
    • 1088, e1
    • N.Y. Yao, and M. O'Donnell SnapShot: The replisome Cell 141 2010 1088 1088, e1
    • (2010) Cell , vol.141 , pp. 1088
    • Yao, N.Y.1    O'Donnell, M.2
  • 10
    • 84871181366 scopus 로고    scopus 로고
    • DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast
    • T. Handa, M. Kanke, T.S. Takahashi, T. Nakagawa, and H. Masukata DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast Mol. Biol. Cell 23 2012 3240 3253
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3240-3253
    • Handa, T.1    Kanke, M.2    Takahashi, T.S.3    Nakagawa, T.4    Masukata, H.5
  • 11
    • 84859980381 scopus 로고    scopus 로고
    • Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis
    • Y.H. Kang, W.C. Galal, A. Farina, I. Tappin, and J. Hurwitz Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis Proc. Natl. Acad. Sci. USA 109 2012 6042 6047
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6042-6047
    • Kang, Y.H.1    Galal, W.C.2    Farina, A.3    Tappin, I.4    Hurwitz, J.5
  • 12
    • 77949354732 scopus 로고    scopus 로고
    • CDK-dependent complex formation between replication proteins Dpb11, Sld2, Pol (epsilon, and GINS in budding yeast
    • S. Muramatsu, K. Hirai, Y.S. Tak, Y. Kamimura, and H. Araki CDK-dependent complex formation between replication proteins Dpb11, Sld2, Pol (epsilon, and GINS in budding yeast Genes Dev. 24 2010 602 612
    • (2010) Genes Dev. , vol.24 , pp. 602-612
    • Muramatsu, S.1    Hirai, K.2    Tak, Y.S.3    Kamimura, Y.4    Araki, H.5
  • 13
    • 77951244549 scopus 로고    scopus 로고
    • Influence of the human cohesion establishment factor Ctf4/AND-1 on DNA replication
    • V.P. Bermudez, A. Farina, I. Tappin, and J. Hurwitz Influence of the human cohesion establishment factor Ctf4/AND-1 on DNA replication J. Biol. Chem. 285 2010 9493 9505
    • (2010) J. Biol. Chem. , vol.285 , pp. 9493-9505
    • Bermudez, V.P.1    Farina, A.2    Tappin, I.3    Hurwitz, J.4
  • 15
    • 0026441119 scopus 로고
    • Evidence that POB1, a Saccharomyces cerevisiae protein that binds to DNA polymerase alpha, acts in DNA metabolism in vivo
    • J. Miles, and T. Formosa Evidence that POB1, a Saccharomyces cerevisiae protein that binds to DNA polymerase alpha, acts in DNA metabolism in vivo Mol. Cell. Biol. 12 1992 5724 5735
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5724-5735
    • Miles, J.1    Formosa, T.2
  • 17
    • 68049100418 scopus 로고    scopus 로고
    • Replisome progression complex links DNA replication to sister chromatid cohesion in Xenopus egg extracts
    • H. Tanaka, Y. Kubota, T. Tsujimura, M. Kumano, H. Masai, and H. Takisawa Replisome progression complex links DNA replication to sister chromatid cohesion in Xenopus egg extracts Genes Cells 14 2009 949 963
    • (2009) Genes Cells , vol.14 , pp. 949-963
    • Tanaka, H.1    Kubota, Y.2    Tsujimura, T.3    Kumano, M.4    Masai, H.5    Takisawa, H.6
  • 18
    • 13744262292 scopus 로고    scopus 로고
    • Mcl1p is a polymerase α replication accessory factor important for S-phase DNA damage survival
    • DOI 10.1128/EC.4.1.166-177.2005
    • D.R. Williams, and J.R. McIntosh Mcl1p is a polymerase alpha replication accessory factor important for S-phase DNA damage survival Eukaryot. Cell 4 2005 166 177 (Pubitemid 40234434)
    • (2005) Eukaryotic Cell , vol.4 , Issue.1 , pp. 166-177
    • Williams, D.R.1    McIntosh, J.R.2
  • 20
    • 53149135030 scopus 로고    scopus 로고
    • Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint
    • H. Lou, M. Komata, Y. Katou, Z. Guan, C.C. Reis, M. Budd, K. Shirahige, and J.L. Campbell Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint Mol. Cell 32 2008 106 117
    • (2008) Mol. Cell , vol.32 , pp. 106-117
    • Lou, H.1    Komata, M.2    Katou, Y.3    Guan, Z.4    Reis, C.C.5    Budd, M.6    Shirahige, K.7    Campbell, J.L.8
  • 22
    • 24044463869 scopus 로고    scopus 로고
    • Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae
    • DOI 10.1016/j.molcel.2005.06.037, PII S1097276505015157
    • S.J. Szyjka, C.J. Viggiani, and O.M. Aparicio Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae Mol. Cell 19 2005 691 697 (Pubitemid 41219444)
    • (2005) Molecular Cell , vol.19 , Issue.5 , pp. 691-697
    • Szyjka, S.J.1    Viggiani, C.J.2    Aparicio, O.M.3
  • 23
    • 24044552287 scopus 로고    scopus 로고
    • Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53
    • DOI 10.1016/j.molcel.2005.07.028, PII S1097276505015133
    • H. Tourrière, G. Versini, V. Cordón-Preciado, C. Alabert, and P. Pasero Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53 Mol. Cell 19 2005 699 706 (Pubitemid 41219445)
    • (2005) Molecular Cell , vol.19 , Issue.5 , pp. 699-706
    • Tourriere, H.1    Versini, G.2    Cordon-Preciado, V.3    Alabert, C.4    Pasero, P.5
  • 24
    • 34948812991 scopus 로고    scopus 로고
    • Mrc1 and Tof1 regulate DNA replication forks in different ways during normal S phase
    • DOI 10.1091/mbc.E07-05-0500
    • B. Hodgson, A. Calzada, and K. Labib Mrc1 and Tof1 regulate DNA replication forks in different ways during normal S phase Mol. Biol. Cell 18 2007 3894 3902 (Pubitemid 47519482)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.10 , pp. 3894-3902
    • Hodgson, B.1    Calzada, A.2    Labib, K.3
  • 25
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement
    • DOI 10.1016/S0092-8674(00)81039-9
    • S. Kim, H.G. Dallmann, C.S. McHenry, and K.J. Marians Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement Cell 84 1996 643 650 (Pubitemid 26071744)
    • (1996) Cell , vol.84 , Issue.4 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 26
    • 70249118531 scopus 로고    scopus 로고
    • The direct binding of Mrc1, a checkpoint mediator, to Mcm6, a replication helicase, is essential for the replication checkpoint against methyl methanesulfonate-induced stress
    • M. Komata, M. Bando, H. Araki, and K. Shirahige The direct binding of Mrc1, a checkpoint mediator, to Mcm6, a replication helicase, is essential for the replication checkpoint against methyl methanesulfonate-induced stress Mol. Cell. Biol. 29 2009 5008 5019
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5008-5019
    • Komata, M.1    Bando, M.2    Araki, H.3    Shirahige, K.4
  • 27
    • 84858053395 scopus 로고    scopus 로고
    • Replisome stability at defective DNA replication forks is independent of S phase checkpoint kinases
    • G. De Piccoli, Y. Katou, T. Itoh, R. Nakato, K. Shirahige, and K. Labib Replisome stability at defective DNA replication forks is independent of S phase checkpoint kinases Mol. Cell 45 2012 696 704
    • (2012) Mol. Cell , vol.45 , pp. 696-704
    • De Piccoli, G.1    Katou, Y.2    Itoh, T.3    Nakato, R.4    Shirahige, K.5    Labib, K.6
  • 28
    • 33646129230 scopus 로고    scopus 로고
    • Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks
    • M. Kanemaki, and K. Labib Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks EMBO J. 25 2006 1753 1763
    • (2006) EMBO J. , vol.25 , pp. 1753-1763
    • Kanemaki, M.1    Labib, K.2
  • 29
    • 0035901555 scopus 로고    scopus 로고
    • Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in saccharomyces cerevisiae
    • DOI 10.1093/emboj/20.8.2097
    • Y. Kamimura, Y.-S. Tak, A. Sugino, and H. Araki Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae EMBO J. 20 2001 2097 2107 (Pubitemid 32397411)
    • (2001) EMBO Journal , vol.20 , Issue.8 , pp. 2097-2107
    • Kamimura, Y.1    Tak, Y.-S.2    Sugino, A.3    Araki, H.4
  • 30
    • 34547730912 scopus 로고    scopus 로고
    • Characterization of a Triple DNA Polymerase Replisome
    • DOI 10.1016/j.molcel.2007.06.019, PII S1097276507004108
    • P. McInerney, A. Johnson, F. Katz, and M. O'Donnell Characterization of a triple DNA polymerase replisome Mol. Cell 27 2007 527 538 (Pubitemid 47238627)
    • (2007) Molecular Cell , vol.27 , Issue.4 , pp. 527-538
    • McInerney, P.1    Johnson, A.2    Katz, F.3    O'Donnell, M.4
  • 32
    • 84873118328 scopus 로고    scopus 로고
    • The RFC Clamp Loader: Structure and Function
    • N.Y. Yao, and M. O'Donnell The RFC Clamp Loader: Structure and Function Subcell. Biochem. 62 2012 259 279
    • (2012) Subcell. Biochem. , vol.62 , pp. 259-279
    • Yao, N.Y.1    O'Donnell, M.2
  • 34
    • 0037847620 scopus 로고    scopus 로고
    • GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast
    • DOI 10.1101/gad.1065903
    • Y. Takayama, Y. Kamimura, M. Okawa, S. Muramatsu, A. Sugino, and H. Araki GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast Genes Dev. 17 2003 1153 1165 (Pubitemid 36534989)
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1153-1165
    • Takayama, Y.1    Kamimura, Y.2    Okawa, M.3    Muramatsu, S.4    Sugino, A.5    Araki, H.6
  • 35
    • 0032529457 scopus 로고    scopus 로고
    • Phosphoesterase domains associated with DNA polymerases of diverse origins
    • DOI 10.1093/nar/26.16.3746
    • L. Aravind, and E.V. Koonin Phosphoesterase domains associated with DNA polymerases of diverse origins Nucleic Acids Res. 26 1998 3746 3752 (Pubitemid 28367981)
    • (1998) Nucleic Acids Research , vol.26 , Issue.16 , pp. 3746-3752
    • Aravind, L.1    Koonin, E.V.2
  • 36
    • 0033941641 scopus 로고    scopus 로고
    • Protein fold recognition using sequence profiles and its application in structural genomics
    • E.V. Koonin, Y.I. Wolf, and L. Aravind Protein fold recognition using sequence profiles and its application in structural genomics Adv. Protein Chem. 54 2000 245 275 (Pubitemid 30458950)
    • (2000) Advances in Protein Chemistry , vol.54 , pp. 245-275
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 37
    • 50849115760 scopus 로고    scopus 로고
    • The solution structure of the amino-terminal domain of human DNA polymerase epsilon subunit B is homologous to C-domains of AAA+ proteins
    • T. Nuutinen, H. Tossavainen, K. Fredriksson, P. Pirilä, P. Permi, H. Pospiech, and J.E. Syvaoja The solution structure of the amino-terminal domain of human DNA polymerase epsilon subunit B is homologous to C-domains of AAA+ proteins Nucleic Acids Res. 36 2008 5102 5110
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5102-5110
    • Nuutinen, T.1    Tossavainen, H.2    Fredriksson, K.3    Pirilä, P.4    Permi, P.5    Pospiech, H.6    Syvaoja, J.E.7
  • 38
    • 34249710254 scopus 로고    scopus 로고
    • A key role for the GINS complex at DNA replication forks
    • DOI 10.1016/j.tcb.2007.04.002, PII S0962892407000852
    • K. Labib, and A. Gambus A key role for the GINS complex at DNA replication forks Trends Cell Biol. 17 2007 271 278 (Pubitemid 46829847)
    • (2007) Trends in Cell Biology , vol.17 , Issue.6 , pp. 271-278
    • Labib, K.1    Gambus, A.2
  • 40
  • 41
    • 34247629049 scopus 로고    scopus 로고
    • Structure of the human GINS complex and its assembly and functional interface in replication initiation
    • DOI 10.1038/nsmb1231, PII NSMB1231
    • K. Kamada, Y. Kubota, T. Arata, Y. Shindo, and F. Hanaoka Structure of the human GINS complex and its assembly and functional interface in replication initiation Nat. Struct. Mol. Biol. 14 2007 388 396 (Pubitemid 46685881)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.5 , pp. 388-396
    • Kamada, K.1    Kubota, Y.2    Arata, T.3    Shindo, Y.4    Hanaoka, F.5
  • 43
    • 73349085934 scopus 로고    scopus 로고
    • An auxin-based degron system for the rapid depletion of proteins in nonplant cells
    • K. Nishimura, T. Fukagawa, H. Takisawa, T. Kakimoto, and M. Kanemaki An auxin-based degron system for the rapid depletion of proteins in nonplant cells Nat. Methods 6 2009 917 922
    • (2009) Nat. Methods , vol.6 , pp. 917-922
    • Nishimura, K.1    Fukagawa, T.2    Takisawa, H.3    Kakimoto, T.4    Kanemaki, M.5
  • 44
    • 84871242841 scopus 로고    scopus 로고
    • The C-terminus of Dpb2 is required for interaction with Pol2 and for cell viability
    • I. Isoz, U. Persson, K. Volkov, and E. Johansson The C-terminus of Dpb2 is required for interaction with Pol2 and for cell viability Nucleic Acids Res. 40 2012 11545 11553
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11545-11553
    • Isoz, I.1    Persson, U.2    Volkov, K.3    Johansson, E.4
  • 45
    • 80051695516 scopus 로고    scopus 로고
    • Studies on human DNA polymerase epsilon and GINS complex and their role in DNA replication
    • V.P. Bermudez, A. Farina, V. Raghavan, I. Tappin, and J. Hurwitz Studies on human DNA polymerase epsilon and GINS complex and their role in DNA replication J. Biol. Chem. 286 2011 28963 28977
    • (2011) J. Biol. Chem. , vol.286 , pp. 28963-28977
    • Bermudez, V.P.1    Farina, A.2    Raghavan, V.3    Tappin, I.4    Hurwitz, J.5
  • 46
    • 33748481354 scopus 로고    scopus 로고
    • The DNA polymerase activity of Pol epsilon holoenzyme is required for rapid and efficient chromosomal DNA replication in Xenopus egg extracts
    • K. Shikata, T. Sasa-Masuda, Y. Okuno, S. Waga, and A. Sugino The DNA polymerase activity of Pol epsilon holoenzyme is required for rapid and efficient chromosomal DNA replication in Xenopus egg extracts BMC Biochem. 7 2006 21
    • (2006) BMC Biochem. , vol.7 , pp. 21
    • Shikata, K.1    Sasa-Masuda, T.2    Okuno, Y.3    Waga, S.4    Sugino, A.5
  • 48
    • 84855427966 scopus 로고    scopus 로고
    • RAD51- and MRE11-dependent reassembly of uncoupled CMG helicase complex at collapsed replication forks
    • Y. Hashimoto, F. Puddu, and V. Costanzo RAD51- and MRE11-dependent reassembly of uncoupled CMG helicase complex at collapsed replication forks Nat. Struct. Mol. Biol. 19 2012 17 24
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 17-24
    • Hashimoto, Y.1    Puddu, F.2    Costanzo, V.3


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