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Volumn 425, Issue 23, 2013, Pages 4820-4836

Assembly and distributive action of an archaeal DNA polymerase holoenzyme

Author keywords

archaeal replication; DNA polymerase holoenzyme; dynamic processivity; PCNA; PIP motif

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARCHAEAL DNA; CELL NUCLEUS ANTIGEN; DNA POLYMERASE; HOLOENZYME; NUCLEOTIDE; REPLICATION FACTOR C;

EID: 84887401200     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.09.003     Document Type: Article
Times cited : (16)

References (78)
  • 1
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • X.P. Kong, R. Onrust, M. O'Donnell, and J. Kuriyan Three-dimensional structure of the beta subunit of E coli DNA polymerase III holoenzyme: a sliding DNA clamp Cell 69 1992 425 437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 2
    • 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
  • 4
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E coli DNA polymerase III
    • D. Jeruzalmi, O. Yurieva, Y. Zhao, M. Young, J. Stewart, and M. Hingorani Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E coli DNA polymerase III Cell 106 2001 417 428
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6
  • 5
    • 0035179213 scopus 로고    scopus 로고
    • Intricacies in ATP-dependent clamp loading: Variations across replication systems
    • M.A. Trakselis, and S.J. Benkovic Intricacies in ATP-dependent clamp loading: variations across replication systems Structure 9 2001 999 1004
    • (2001) Structure , vol.9 , pp. 999-1004
    • Trakselis, M.A.1    Benkovic, S.J.2
  • 6
    • 63549113890 scopus 로고    scopus 로고
    • Loading clamps for DNA replication and repair
    • L.B. Bloom Loading clamps for DNA replication and repair DNA Repair (Amst) 8 2009 570 578
    • (2009) DNA Repair (Amst) , vol.8 , pp. 570-578
    • Bloom, L.B.1
  • 7
    • 0035902595 scopus 로고    scopus 로고
    • Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer
    • M.A. Trakselis, S.C. Alley, E. Abel-Santos, and S.J. Benkovic Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer Proc Natl Acad Sci USA 98 2001 8368 8375
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8368-8375
    • Trakselis, M.A.1    Alley, S.C.2    Abel-Santos, E.3    Benkovic, S.J.4
  • 8
    • 33745625118 scopus 로고    scopus 로고
    • Single-molecule investigation of the T4 bacteriophage DNA polymerase holoenzyme: Multiple pathways of holoenzyme formation
    • R.D. Smiley, Z. Zhuang, S.J. Benkovic, and G.G. Hammes Single-molecule investigation of the T4 bacteriophage DNA polymerase holoenzyme: multiple pathways of holoenzyme formation Biochemistry 45 2006 7990 7997
    • (2006) Biochemistry , vol.45 , pp. 7990-7997
    • Smiley, R.D.1    Zhuang, Z.2    Benkovic, S.J.3    Hammes, G.G.4
  • 9
    • 0037436329 scopus 로고    scopus 로고
    • Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme
    • M.A. Trakselis, A.J. Berdis, and S.J. Benkovic Examination of the role of the clamp-loader and ATP hydrolysis in the formation of the bacteriophage T4 polymerase holoenzyme J Mol Biol 326 2003 435 451
    • (2003) J Mol Biol , vol.326 , pp. 435-451
    • Trakselis, M.A.1    Berdis, A.J.2    Benkovic, S.J.3
  • 10
    • 70450265205 scopus 로고    scopus 로고
    • A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of beta clamp binding by the Escherichia coli gamma complex clamp loader
    • J.A. Thompson, C.O. Paschall, M. O'Donnell, and L.B. Bloom A slow ATP-induced conformational change limits the rate of DNA binding but not the rate of beta clamp binding by the Escherichia coli gamma complex clamp loader J Biol Chem 284 2009 32147 32157
    • (2009) J Biol Chem , vol.284 , pp. 32147-32157
    • Thompson, J.A.1    Paschall, C.O.2    O'Donnell, M.3    Bloom, L.B.4
  • 12
    • 84872342442 scopus 로고    scopus 로고
    • The beta sliding clamp closes around DNA prior to release by the Escherichia coli clamp loader gamma complex
    • J.N. Hayner, and L.B. Bloom The beta sliding clamp closes around DNA prior to release by the Escherichia coli clamp loader gamma complex J Biol Chem 288 2013 1162 1170
    • (2013) J Biol Chem , vol.288 , pp. 1162-1170
    • Hayner, J.N.1    Bloom, L.B.2
  • 13
    • 84863393472 scopus 로고    scopus 로고
    • Replication factor C is a more effective proliferating cell nuclear antigen (PCNA) opener than the checkpoint clamp loader, Rad24-RFC
    • J.A. Thompson, M.R. Marzahn, M. O'Donnell, and L.B. Bloom Replication factor C is a more effective proliferating cell nuclear antigen (PCNA) opener than the checkpoint clamp loader, Rad24-RFC J Biol Chem 287 2012 2203 2209
    • (2012) J Biol Chem , vol.287 , pp. 2203-2209
    • Thompson, J.A.1    Marzahn, M.R.2    O'Donnell, M.3    Bloom, L.B.4
  • 14
    • 33745187598 scopus 로고    scopus 로고
    • Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C
    • N.Y. Yao, A. Johnson, G.D. Bowman, J. Kuriyan, and M. O'Donnell Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C J Biol Chem 281 2006 17528 17539
    • (2006) J Biol Chem , vol.281 , pp. 17528-17539
    • Yao, N.Y.1    Johnson, A.2    Bowman, G.D.3    Kuriyan, J.4    O'Donnell, M.5
  • 15
    • 0035860719 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen
    • X.V. Gomes, and P.M. Burgers ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen J Biol Chem 276 2001 34768 34775
    • (2001) J Biol Chem , vol.276 , pp. 34768-34775
    • Gomes, X.V.1    Burgers, P.M.2
  • 16
    • 84883212945 scopus 로고    scopus 로고
    • Stepwise assembly of the human replicative polymerase holoenzyme
    • M. Hedglin, S.K. Perumal, Z. Hu, and S. Benkovic Stepwise assembly of the human replicative polymerase holoenzyme Elife 2 2013 e00278
    • (2013) Elife , vol.2 , pp. 00278
    • Hedglin, M.1    Perumal, S.K.2    Hu, Z.3    Benkovic, S.4
  • 17
    • 34547730912 scopus 로고    scopus 로고
    • Characterization of a triple DNA polymerase replisome
    • P. McInerney, A. Johnson, F. Katz, and M. O'Donnell Characterization of a triple DNA polymerase replisome Mol Cell 27 2007 527 538
    • (2007) Mol Cell , vol.27 , pp. 527-538
    • McInerney, P.1    Johnson, A.2    Katz, F.3    O'Donnell, M.4
  • 19
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res 9 1999 27 43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 20
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • J. Turner, M.M. Hingorani, Z. Kelman, and M. O'Donnell The internal workings of a DNA polymerase clamp-loading machine EMBO J 18 1999 771 783
    • (1999) EMBO J , vol.18 , pp. 771-783
    • Turner, J.1    Hingorani, M.M.2    Kelman, Z.3    O'Donnell, M.4
  • 21
    • 0032544708 scopus 로고    scopus 로고
    • ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme
    • M.M. Hingorani, and M. O'Donnell ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme J Biol Chem 273 1998 24550 24563
    • (1998) J Biol Chem , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 22
    • 0032544709 scopus 로고    scopus 로고
    • Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Escherichia coli DNA polymerase III onto DNA
    • J.G. Bertram, L.B. Bloom, J. Turner, M. O'Donnell, J.M. Beechem, and M.F. Goodman Pre-steady state analysis of the assembly of wild type and mutant circular clamps of Escherichia coli DNA polymerase III onto DNA J Biol Chem 273 1998 24564 24574
    • (1998) J Biol Chem , vol.273 , pp. 24564-24574
    • Bertram, J.G.1    Bloom, L.B.2    Turner, J.3    O'Donnell, M.4    Beechem, J.M.5    Goodman, M.F.6
  • 23
    • 0033568602 scopus 로고    scopus 로고
    • Division of labor - Sequential ATP hydrolysis drives assembly of a DNA polymerase sliding clamp around DNA
    • M.M. Hingorani, L.B. Bloom, M.F. Goodman, and M. O'Donnell Division of labor - sequential ATP hydrolysis drives assembly of a DNA polymerase sliding clamp around DNA EMBO J 18 1999 5131 5144
    • (1999) EMBO J , vol.18 , pp. 5131-5144
    • Hingorani, M.M.1    Bloom, L.B.2    Goodman, M.F.3    O'Donnell, M.4
  • 24
    • 80052343292 scopus 로고    scopus 로고
    • Polymerase chaperoning and multiple ATPase sites enable the E coli DNA polymerase III holoenzyme to rapidly form initiation complexes
    • C.D. Downey, E. Crooke, and C.S. McHenry Polymerase chaperoning and multiple ATPase sites enable the E coli DNA polymerase III holoenzyme to rapidly form initiation complexes J Mol Biol 412 2011 340 353
    • (2011) J Mol Biol , vol.412 , pp. 340-353
    • Downey, C.D.1    Crooke, E.2    McHenry, C.S.3
  • 25
    • 0032102260 scopus 로고    scopus 로고
    • Clamping down on clamps and clamp loaders - The eukaryotic replication factor C
    • R. Mossi, and U. Hubscher 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
  • 26
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • G.D. Bowman, M. O'Donnell, and J. Kuriyan Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex Nature 429 2004 724 730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 27
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma complex of E coli DNA polymerase III
    • D. Jeruzalmi, M. O'Donnell, and J. Kuriyan Crystal structure of the processivity clamp loader gamma complex of E coli DNA polymerase III Cell 106 2001 429 441
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 28
    • 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
  • 29
    • 0032031972 scopus 로고    scopus 로고
    • PCNA binding through a conserved motif
    • E. Warbrick PCNA binding through a conserved motif BioEssays 20 1998 195 199
    • (1998) BioEssays , vol.20 , pp. 195-199
    • Warbrick, E.1
  • 30
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • J.M. Gulbis, Z. Kelman, J. Hurwitz, M. O'Donnell, and J. Kuriyan Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA Cell 87 1996 297 306
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 31
    • 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
  • 32
    • 0035949599 scopus 로고    scopus 로고
    • A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems
    • B.P. Dalrymple, K. Kongsuwan, G. Wijffels, N.E. Dixon, and P.A. Jennings A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems Proc Natl Acad Sci USA 98 2001 11627 11632
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11627-11632
    • Dalrymple, B.P.1    Kongsuwan, K.2    Wijffels, G.3    Dixon, N.E.4    Jennings, P.A.5
  • 33
    • 2442507194 scopus 로고    scopus 로고
    • Inhibition of protein interactions with the beta 2 sliding clamp of Escherichia coli DNA polymerase III by peptides from beta 2-binding proteins
    • G. Wijffels, B.P. Dalrymple, P. Prosselkov, K. Kongsuwan, V.C. Epa, and P.E. Lilley Inhibition of protein interactions with the beta 2 sliding clamp of Escherichia coli DNA polymerase III by peptides from beta 2-binding proteins Biochemistry 43 2004 5661 5671
    • (2004) Biochemistry , vol.43 , pp. 5661-5671
    • Wijffels, G.1    Dalrymple, B.P.2    Prosselkov, P.3    Kongsuwan, K.4    Epa, V.C.5    Lilley, P.E.6
  • 34
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Y. Shamoo, and T.A. Steitz Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex Cell 99 1999 155 166
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 35
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • I. Dionne, R.K. Nookala, S.P. Jackson, A.J. Doherty, and S.D. Bell A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus Mol Cell 11 2003 275 282
    • (2003) Mol Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.K.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 36
    • 1942503398 scopus 로고    scopus 로고
    • Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader
    • A. Seybert, and D.B. Wigley Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader EMBO J 23 2004 1360 1371
    • (2004) EMBO J , vol.23 , pp. 1360-1371
    • Seybert, A.1    Wigley, D.B.2
  • 37
    • 0037109208 scopus 로고    scopus 로고
    • Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus
    • A. Seybert, D.J. Scott, S. Scaife, M.R. Singleton, and D.B. Wigley Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus Nucleic Acids Res 30 2002 4329 4338
    • (2002) Nucleic Acids Res , vol.30 , pp. 4329-4338
    • Seybert, A.1    Scott, D.J.2    Scaife, S.3    Singleton, M.R.4    Wigley, D.B.5
  • 38
    • 25444480278 scopus 로고    scopus 로고
    • Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis
    • T. Miyata, H. Suzuki, T. Oyama, K. Mayanagi, Y. Ishino, and K. Morikawa Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis Proc Natl Acad Sci USA 102 2005 13795 13800
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13795-13800
    • Miyata, T.1    Suzuki, H.2    Oyama, T.3    Mayanagi, K.4    Ishino, Y.5    Morikawa, K.6
  • 40
    • 69449095740 scopus 로고    scopus 로고
    • Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression
    • N.Y. Yao, R.E. Georgescu, J. Finkelstein, and M.E. O'Donnell Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression Proc Natl Acad Sci USA 106 2009 13236 13241
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13236-13241
    • Yao, N.Y.1    Georgescu, R.E.2    Finkelstein, J.3    O'Donnell, M.E.4
  • 41
    • 84869049178 scopus 로고    scopus 로고
    • The human lagging strand DNA polymerase delta holoenzyme is distributive
    • Z. Hu, S.K. Perumal, H. Yue, and S.J. Benkovic The human lagging strand DNA polymerase delta holoenzyme is distributive J Biol Chem 287 2012 38442 38448
    • (2012) J Biol Chem , vol.287 , pp. 38442-38448
    • Hu, Z.1    Perumal, S.K.2    Yue, H.3    Benkovic, S.J.4
  • 42
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • P.M. Burgers Polymerase dynamics at the eukaryotic DNA replication fork J Biol Chem 284 2009 4041 4045
    • (2009) J Biol Chem , vol.284 , pp. 4041-4045
    • Burgers, P.M.1
  • 43
    • 57649139149 scopus 로고    scopus 로고
    • DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA
    • L.D. Langston, and M. O'Donnell DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA J Biol Chem 283 2008 29522 29531
    • (2008) J Biol Chem , vol.283 , pp. 29522-29531
    • Langston, L.D.1    O'Donnell, M.2
  • 44
    • 84866409927 scopus 로고    scopus 로고
    • Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity
    • H.K. Lin, S.F. Chase, T.M. Laue, L. Jen-Jacobson, and M.A. Trakselis Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity Biochemistry 51 2012 7367 7382
    • (2012) Biochemistry , vol.51 , pp. 7367-7382
    • Lin, H.K.1    Chase, S.F.2    Laue, T.M.3    Jen-Jacobson, L.4    Trakselis, M.A.5
  • 45
    • 0035093865 scopus 로고    scopus 로고
    • Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus
    • I.K. Cann, S. Ishino, M. Yuasa, H. Daiyasu, H. Toh, and Y. Ishino Biochemical analysis of replication factor C from the hyperthermophilic archaeon Pyrococcus furiosus J Bacteriol 183 2001 2614 2623
    • (2001) J Bacteriol , vol.183 , pp. 2614-2623
    • Cann, I.K.1    Ishino, S.2    Yuasa, M.3    Daiyasu, H.4    Toh, H.5    Ishino, Y.6
  • 48
    • 0028033533 scopus 로고
    • The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme
    • K.J. Hacker, and B.M. Alberts The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme J Biol Chem 269 1994 24209 24220
    • (1994) J Biol Chem , vol.269 , pp. 24209-24220
    • Hacker, K.J.1    Alberts, B.M.2
  • 49
    • 7944222972 scopus 로고    scopus 로고
    • Insights into DNA replication: The crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus
    • C. Savino, L. Federici, K.A. Johnson, B. Vallone, V. Nastopoulos, and M. Rossi Insights into DNA replication: the crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus Structure 12 2004 2001 2008
    • (2004) Structure , vol.12 , pp. 2001-2008
    • Savino, C.1    Federici, L.2    Johnson, K.A.3    Vallone, B.4    Nastopoulos, V.5    Rossi, M.6
  • 50
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys J 80 2001 2946 2953
    • (2001) Biophys J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 51
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • D.I. Svergun Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys J 76 1999 2879 2886
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 52
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J Appl Crystallogr 25 1992 495 503
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 53
    • 0028357737 scopus 로고
    • Coordination of leading and lagging strand DNA synthesis at the replication fork of bacteriophage T7
    • Z. Debyser, S. Tabor, and C.C. Richardson Coordination of leading and lagging strand DNA synthesis at the replication fork of bacteriophage T7 Cell 77 1994 157 166
    • (1994) Cell , vol.77 , pp. 157-166
    • Debyser, Z.1    Tabor, S.2    Richardson, C.C.3
  • 54
    • 0035800866 scopus 로고    scopus 로고
    • Conditional coupling of leading-strand and lagging-strand DNA synthesis at bacteriophage T4 replication forks
    • F.A. Kadyrov, and J.W. Drake Conditional coupling of leading-strand and lagging-strand DNA synthesis at bacteriophage T4 replication forks J Biol Chem 276 2001 29559 29566
    • (2001) J Biol Chem , vol.276 , pp. 29559-29566
    • Kadyrov, F.A.1    Drake, J.W.2
  • 55
    • 0029839057 scopus 로고    scopus 로고
    • Tau Couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork
    • S. Kim, H.G. Dallmann, C.S. McHenry, and K.J. Marians tau Couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork J Biol Chem 271 1996 21406 21412
    • (1996) J Biol Chem , vol.271 , pp. 21406-21412
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 57
    • 79952746781 scopus 로고    scopus 로고
    • Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange
    • J.J. Loparo, A.W. Kulczyk, C.C. Richardson, and A.M. van Oijen Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange Proc Natl Acad Sci USA 108 2011 3584 3589
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3584-3589
    • Loparo, J.J.1    Kulczyk, A.W.2    Richardson, C.C.3    Van Oijen, A.M.4
  • 58
    • 45549085521 scopus 로고    scopus 로고
    • A dynamic polymerase exchange with Escherichia coli DNA polymerase IV replacing DNA polymerase III on the sliding clamp
    • A. Furukohri, M.F. Goodman, and H. Maki A dynamic polymerase exchange with Escherichia coli DNA polymerase IV replacing DNA polymerase III on the sliding clamp J Biol Chem 283 2008 11260 11269
    • (2008) J Biol Chem , vol.283 , pp. 11260-11269
    • Furukohri, A.1    Goodman, M.F.2    Maki, H.3
  • 59
    • 24944543952 scopus 로고    scopus 로고
    • A sliding-clamp toolbelt binds high- and low-fidelity DNA polymerases simultaneously
    • C. Indiani, P. McInerney, R. Georgescu, M.F. Goodman, and M. O'Donnell 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
  • 60
    • 0034696523 scopus 로고    scopus 로고
    • Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly
    • S.C. Alley, E. Abel-Santos, and S.J. Benkovic Tracking sliding clamp opening and closing during bacteriophage T4 DNA polymerase holoenzyme assembly Biochemistry 39 2000 3076 3090
    • (2000) Biochemistry , vol.39 , pp. 3076-3090
    • Alley, S.C.1    Abel-Santos, E.2    Benkovic, S.J.3
  • 61
    • 78650557325 scopus 로고    scopus 로고
    • Stepwise loading of yeast clamp revealed by ensemble and single-molecule studies
    • R. Kumar, V.C. Nashine, P.P. Mishra, S.J. Benkovic, and T.H. Lee Stepwise loading of yeast clamp revealed by ensemble and single-molecule studies Proc Natl Acad Sci USA 107 2010 19736 19741
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19736-19741
    • Kumar, R.1    Nashine, V.C.2    Mishra, P.P.3    Benkovic, S.J.4    Lee, T.H.5
  • 63
    • 0035860694 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA
    • X.V. Gomes, S.L. Schmidt, and P.M. Burgers ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA J Biol Chem 276 2001 34776 34783
    • (2001) J Biol Chem , vol.276 , pp. 34776-34783
    • Gomes, X.V.1    Schmidt, S.L.2    Burgers, P.M.3
  • 64
    • 64649100384 scopus 로고    scopus 로고
    • Mechanism of ATP-driven PCNA clamp loading by S cerevisiae RFC
    • S. Chen, M.K. Levin, M. Sakato, Y. Zhou, and M.M. Hingorani Mechanism of ATP-driven PCNA clamp loading by S cerevisiae RFC J Mol Biol 388 2009 431 442
    • (2009) J Mol Biol , vol.388 , pp. 431-442
    • Chen, S.1    Levin, M.K.2    Sakato, M.3    Zhou, Y.4    Hingorani, M.M.5
  • 65
    • 40549087271 scopus 로고    scopus 로고
    • On the mechanism of loading the PCNA sliding clamp by RFC
    • I. Dionne, N.J. Brown, R. Woodgate, and S.D. Bell On the mechanism of loading the PCNA sliding clamp by RFC Mol Microbiol 68 2008 216 222
    • (2008) Mol Microbiol , vol.68 , pp. 216-222
    • Dionne, I.1    Brown, N.J.2    Woodgate, R.3    Bell, S.D.4
  • 66
    • 70149109582 scopus 로고    scopus 로고
    • Temporal correlation of DNA binding, ATP hydrolysis, and clamp release in the clamp loading reaction catalyzed by the Escherichia coli gamma complex
    • S.G. Anderson, J.A. Thompson, C.O. Paschall, M. O'Donnell, and L.B. Bloom Temporal correlation of DNA binding, ATP hydrolysis, and clamp release in the clamp loading reaction catalyzed by the Escherichia coli gamma complex Biochemistry 48 2009 8516 8527
    • (2009) Biochemistry , vol.48 , pp. 8516-8527
    • Anderson, S.G.1    Thompson, J.A.2    Paschall, C.O.3    O'Donnell, M.4    Bloom, L.B.5
  • 67
    • 0030064447 scopus 로고    scopus 로고
    • Dual role of the 44/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex
    • B.F. Kaboord, and S.J. Benkovic Dual role of the 44/62 protein as a matchmaker protein and DNA polymerase chaperone during assembly of the bacteriophage T4 holoenzyme complex Biochemistry 35 1996 1084 1092
    • (1996) Biochemistry , vol.35 , pp. 1084-1092
    • Kaboord, B.F.1    Benkovic, S.J.2
  • 68
    • 58449104506 scopus 로고    scopus 로고
    • Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA
    • G. Xing, K. Kirouac, Y.J. Shin, S.D. Bell, and H. Ling Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA Mol Microbiol 71 2009 678 691
    • (2009) Mol Microbiol , vol.71 , pp. 678-691
    • Xing, G.1    Kirouac, K.2    Shin, Y.J.3    Bell, S.D.4    Ling, H.5
  • 71
    • 84871385554 scopus 로고    scopus 로고
    • Rings in the extreme: PCNA interactions and adaptations in the archaea
    • J.A. Winter, and K.A. Bunting Rings in the extreme: PCNA interactions and adaptations in the archaea Archaea 2012 2012 951010
    • (2012) Archaea , vol.2012 , pp. 951010
    • Winter, J.A.1    Bunting, K.A.2
  • 72
    • 79952164207 scopus 로고    scopus 로고
    • Architecture of the DNA polymerase B-proliferating cell nuclear antigen (PCNA)-DNA ternary complex
    • K. Mayanagi, S. Kiyonari, H. Nishida, M. Saito, D. Kohda, and Y. Ishino Architecture of the DNA polymerase B-proliferating cell nuclear antigen (PCNA)-DNA ternary complex Proc Natl Acad Sci USA 2011 1845 1849
    • (2011) Proc Natl Acad Sci USA , pp. 1845-1849
    • Mayanagi, K.1    Kiyonari, S.2    Nishida, H.3    Saito, M.4    Kohda, D.5    Ishino, Y.6
  • 73
    • 73949096397 scopus 로고    scopus 로고
    • Structural determinant for switching between the polymerase and exonuclease modes in the PCNA-replicative DNA polymerase complex
    • H. Nishida, K. Mayanagi, S. Kiyonari, Y. Sato, T. Oyama, and Y. Ishino Structural determinant for switching between the polymerase and exonuclease modes in the PCNA-replicative DNA polymerase complex Proc Natl Acad Sci USA 106 2009 20693 20698
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20693-20698
    • Nishida, H.1    Mayanagi, K.2    Kiyonari, S.3    Sato, Y.4    Oyama, T.5    Ishino, Y.6
  • 74
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • F.W. Studier Protein production by auto-induction in high density shaking cultures Protein Expression Purif 41 2005 207 234
    • (2005) Protein Expression Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 75
    • 84875731470 scopus 로고    scopus 로고
    • Novel interaction of the bacterial-like DnaG primase with the MCM helicase in archaea
    • R.J. Bauer, B.W. Graham, and M.A. Trakselis Novel interaction of the bacterial-like DnaG primase with the MCM helicase in archaea J Mol Biol 425 2013 1259 1273
    • (2013) J Mol Biol , vol.425 , pp. 1259-1273
    • Bauer, R.J.1    Graham, B.W.2    Trakselis, M.A.3
  • 76
    • 84857853904 scopus 로고    scopus 로고
    • Kinetics and fidelity of polymerization by DNA polymerase III from Sulfolobus solfataricus
    • R.J. Bauer, M.T. Begley, and M.A. Trakselis Kinetics and fidelity of polymerization by DNA polymerase III from Sulfolobus solfataricus Biochemistry 51 2012 1996 2007
    • (2012) Biochemistry , vol.51 , pp. 1996-2007
    • Bauer, R.J.1    Begley, M.T.2    Trakselis, M.A.3
  • 77
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • A.T. McGeoch, M.A. Trakselis, R.A. Laskey, and S.D. Bell Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism Nat Struct Mol Biol 12 2005 756 762
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 756-762
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 78
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J Appl Crystallogr 36 2003 860 864
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2


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