메뉴 건너뛰기




Volumn 23, Issue 1, 2013, Pages 144-153

A structural framework for replication origin opening by AAA+ initiation factors

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DNAB HELICASE; HELICASE; HELIX LOOP HELIX PROTEIN; INITIATION FACTOR; REPLICATION INITIATOR PROTEIN DNAA; SINGLE STRANDED DNA;

EID: 84873526234     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2012.11.012     Document Type: Review
Times cited : (45)

References (83)
  • 1
    • 45849087274 scopus 로고    scopus 로고
    • AAA+ ATPases in the initiation of DNA replication
    • Duderstadt K.E., Berger J.M. AAA+ ATPases in the initiation of DNA replication. Crit Rev Biochem Mol Biol 2008, 43:163-187.
    • (2008) Crit Rev Biochem Mol Biol , vol.43 , pp. 163-187
    • Duderstadt, K.E.1    Berger, J.M.2
  • 2
    • 14544277626 scopus 로고    scopus 로고
    • Origin recognition and the chromosome cycle
    • Stillman B. Origin recognition and the chromosome cycle. FEBS Lett 2005, 579:877-884.
    • (2005) FEBS Lett , vol.579 , pp. 877-884
    • Stillman, B.1
  • 3
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: controlling the initiation of bacterial DNA replication and more
    • Kaguni J.M. DnaA: controlling the initiation of bacterial DNA replication and more. Annu Rev Microbiol 2006, 60:351-375.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 351-375
    • Kaguni, J.M.1
  • 4
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: components and dynamics at the replication fork
    • Johnson A., O'Donnell M. Cellular DNA replicases: components and dynamics at the replication fork. Annu Rev Biochem 2005, 74:283-315.
    • (2005) Annu Rev Biochem , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 5
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 1999, 9:27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 6
    • 0024095899 scopus 로고
    • Localized melting and structural changes in the SV40 origin of replication induced by T-antigen
    • Borowiec J.A., Hurwitz J. Localized melting and structural changes in the SV40 origin of replication induced by T-antigen. EMBO J 1988, 7:3149-3158.
    • (1988) EMBO J , vol.7 , pp. 3149-3158
    • Borowiec, J.A.1    Hurwitz, J.2
  • 7
    • 0023658349 scopus 로고
    • ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu K., Bramhill D., Kornberg A. ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell 1987, 50:259-265.
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 8
    • 80052215701 scopus 로고    scopus 로고
    • Mechanistic analysis of local ori melting and helicase assembly by the papillomavirus E1 protein
    • Schuck S., Stenlund A. Mechanistic analysis of local ori melting and helicase assembly by the papillomavirus E1 protein. Mol Cell 2011, 43:776-787.
    • (2011) Mol Cell , vol.43 , pp. 776-787
    • Schuck, S.1    Stenlund, A.2
  • 9
    • 80054029342 scopus 로고    scopus 로고
    • DNA stretching by bacterial initiators promotes replication origin opening
    • Duderstadt K.E., Chuang K., Berger J.M. DNA stretching by bacterial initiators promotes replication origin opening. Nature 2011, 478:209-213.
    • (2011) Nature , vol.478 , pp. 209-213
    • Duderstadt, K.E.1    Chuang, K.2    Berger, J.M.3
  • 10
    • 10944235448 scopus 로고    scopus 로고
    • ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication
    • Bowers J.L., Randell J.C., Chen S., Bell S.P. ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication. Mol Cell 2004, 16:967-978.
    • (2004) Mol Cell , vol.16 , pp. 967-978
    • Bowers, J.L.1    Randell, J.C.2    Chen, S.3    Bell, S.P.4
  • 11
    • 0031002795 scopus 로고    scopus 로고
    • Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex
    • Klemm R.D., Austin R.J., Bell S.P. Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex. Cell 1997, 88:493-502.
    • (1997) Cell , vol.88 , pp. 493-502
    • Klemm, R.D.1    Austin, R.J.2    Bell, S.P.3
  • 12
    • 33645513776 scopus 로고    scopus 로고
    • A structural role for ATP in the formation and stability of the human origin recognition complex
    • Ranjan A., Gossen M. A structural role for ATP in the formation and stability of the human origin recognition complex. Proc Natl Acad Sci U S A 2006, 103:4864-4869.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4864-4869
    • Ranjan, A.1    Gossen, M.2
  • 13
    • 36148977594 scopus 로고    scopus 로고
    • ATP-dependent assembly of the human origin recognition complex
    • Siddiqui K., Stillman B. ATP-dependent assembly of the human origin recognition complex. J Biol Chem 2007, 282:32370-32383.
    • (2007) J Biol Chem , vol.282 , pp. 32370-32383
    • Siddiqui, K.1    Stillman, B.2
  • 14
    • 0032110626 scopus 로고    scopus 로고
    • Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders
    • Perkins G., Diffley J.F. Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders. Mol Cell 1998, 2:23-32.
    • (1998) Mol Cell , vol.2 , pp. 23-32
    • Perkins, G.1    Diffley, J.F.2
  • 15
    • 0023664708 scopus 로고
    • In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome
    • Funnell B.E., Baker T.A., Kornberg A. In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. J Biol Chem 1987, 262:10327-10334.
    • (1987) J Biol Chem , vol.262 , pp. 10327-10334
    • Funnell, B.E.1    Baker, T.A.2    Kornberg, A.3
  • 16
    • 0027381536 scopus 로고
    • Replicatively active complexes of DnaA protein and the Escherichia coli chromosomal origin observed in the electron microscope
    • Crooke E., Thresher R., Hwang D.S., Griffith J., Kornberg A. Replicatively active complexes of DnaA protein and the Escherichia coli chromosomal origin observed in the electron microscope. J Mol Biol 1993, 233:16-24.
    • (1993) J Mol Biol , vol.233 , pp. 16-24
    • Crooke, E.1    Thresher, R.2    Hwang, D.S.3    Griffith, J.4    Kornberg, A.5
  • 17
    • 22844437103 scopus 로고    scopus 로고
    • Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family
    • Kawakami H., Keyamura K., Katayama T. Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family. J Biol Chem 2005, 280:27420-27430.
    • (2005) J Biol Chem , vol.280 , pp. 27420-27430
    • Kawakami, H.1    Keyamura, K.2    Katayama, T.3
  • 18
    • 0030035666 scopus 로고    scopus 로고
    • Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli
    • Margulies C., Kaguni J.M. Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli. J Biol Chem 1996, 271:17035-17040.
    • (1996) J Biol Chem , vol.271 , pp. 17035-17040
    • Margulies, C.1    Kaguni, J.M.2
  • 19
    • 76949086750 scopus 로고    scopus 로고
    • Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC
    • Katayama T., Ozaki S., Keyamura K., Fujimitsu K. Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC. Nat Rev Microbiol 2010, 8:163-170.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 163-170
    • Katayama, T.1    Ozaki, S.2    Keyamura, K.3    Fujimitsu, K.4
  • 21
    • 0024786678 scopus 로고
    • The DNA unwinding element: a novel, cis-acting component that facilitates opening of the Escherichia coli replication origin
    • Kowalski D., Eddy M.J. The DNA unwinding element: a novel, cis-acting component that facilitates opening of the Escherichia coli replication origin. EMBO J 1989, 8:4335-4344.
    • (1989) EMBO J , vol.8 , pp. 4335-4344
    • Kowalski, D.1    Eddy, M.J.2
  • 22
    • 0024284091 scopus 로고
    • Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
    • Bramhill D., Kornberg A. Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell 1988, 52:743-755.
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 23
    • 0029030019 scopus 로고
    • The DNA binding domain of the initiator protein DnaA
    • Roth A., Messer W. The DNA binding domain of the initiator protein DnaA. EMBO J 1995, 14:2106-2111.
    • (1995) EMBO J , vol.14 , pp. 2106-2111
    • Roth, A.1    Messer, W.2
  • 24
    • 0030823757 scopus 로고    scopus 로고
    • Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity
    • Sutton M.D., Kaguni J.M. Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity. J Biol Chem 1997, 272:23017-23024.
    • (1997) J Biol Chem , vol.272 , pp. 23017-23024
    • Sutton, M.D.1    Kaguni, J.M.2
  • 27
    • 84857873014 scopus 로고    scopus 로고
    • Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation
    • Ozaki S., Katayama T. Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation. Nucleic Acids Res 2012, 40:1648-1665.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1648-1665
    • Ozaki, S.1    Katayama, T.2
  • 28
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 2004, 146:11-31.
    • (2004) J Struct Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 29
    • 13844254123 scopus 로고    scopus 로고
    • Binding and unwinding: SF3 viral helicases
    • Hickman A.B., Dyda F. Binding and unwinding: SF3 viral helicases. Curr Opin Struct Biol 2005, 15:77-85.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 77-85
    • Hickman, A.B.1    Dyda, F.2
  • 31
    • 0037086545 scopus 로고    scopus 로고
    • Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex
    • Enemark E.J., Stenlund A., Joshua-Tor L. Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex. EMBO J 2002, 21:1487-1496.
    • (2002) EMBO J , vol.21 , pp. 1487-1496
    • Enemark, E.J.1    Stenlund, A.2    Joshua-Tor, L.3
  • 32
    • 27644484567 scopus 로고    scopus 로고
    • Assembly of a double hexameric helicase
    • Schuck S., Stenlund A. Assembly of a double hexameric helicase. Mol Cell 2005, 20:377-389.
    • (2005) Mol Cell , vol.20 , pp. 377-389
    • Schuck, S.1    Stenlund, A.2
  • 33
    • 0033988190 scopus 로고    scopus 로고
    • Large T-antigen double hexamers imaged at the simian virus 40 origin of replication
    • Valle M., Gruss C., Halmer L., Carazo J.M., Donate L.E. Large T-antigen double hexamers imaged at the simian virus 40 origin of replication. Mol Cell Biol 2000, 20:34-41.
    • (2000) Mol Cell Biol , vol.20 , pp. 34-41
    • Valle, M.1    Gruss, C.2    Halmer, L.3    Carazo, J.M.4    Donate, L.E.5
  • 34
    • 0025613266 scopus 로고
    • Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator
    • Mohr I.J., Clark R., Sun S., Androphy E.J., MacPherson P., Botchan M.R. Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator. Science (New York, NY) 1990, 250:1694-1699.
    • (1990) Science (New York, NY) , vol.250 , pp. 1694-1699
    • Mohr, I.J.1    Clark, R.2    Sun, S.3    Androphy, E.J.4    MacPherson, P.5    Botchan, M.R.6
  • 35
    • 0029617680 scopus 로고
    • Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro
    • Sedman J., Stenlund A. Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro. EMBO J 1995, 14:6218-6228.
    • (1995) EMBO J , vol.14 , pp. 6218-6228
    • Sedman, J.1    Stenlund, A.2
  • 36
    • 0026607331 scopus 로고
    • ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex
    • Bell S.P., Stillman B. ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex. Nature 1992, 357:128-134.
    • (1992) Nature , vol.357 , pp. 128-134
    • Bell, S.P.1    Stillman, B.2
  • 37
    • 0026550902 scopus 로고
    • Protein-DNA interactions at a yeast replication origin
    • Diffley J.F., Cocker J.H. Protein-DNA interactions at a yeast replication origin. Nature 1992, 357:169-172.
    • (1992) Nature , vol.357 , pp. 169-172
    • Diffley, J.F.1    Cocker, J.H.2
  • 38
    • 84863296793 scopus 로고    scopus 로고
    • Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy
    • Sun J., Kawakami H., Zech J., Speck C., Stillman B., Li H. Cdc6-induced conformational changes in ORC bound to origin DNA revealed by cryo-electron microscopy. Structure 2012, 20:534-544.
    • (2012) Structure , vol.20 , pp. 534-544
    • Sun, J.1    Kawakami, H.2    Zech, J.3    Speck, C.4    Stillman, B.5    Li, H.6
  • 40
    • 0035902562 scopus 로고    scopus 로고
    • ATP bound to the origin recognition complex is important for preRC formation
    • Klemm R.D., Bell S.P. ATP bound to the origin recognition complex is important for preRC formation. Proc Natl Acad Sci U S A 2001, 98:8361-8367.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8361-8367
    • Klemm, R.D.1    Bell, S.P.2
  • 41
    • 0034282727 scopus 로고    scopus 로고
    • Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding
    • Lee D.G., Makhov A.M., Klemm R.D., Griffith J.D., Bell S.P. Regulation of origin recognition complex conformation and ATPase activity: differential effects of single-stranded and double-stranded DNA binding. EMBO J 2000, 19:4774-4782.
    • (2000) EMBO J , vol.19 , pp. 4774-4782
    • Lee, D.G.1    Makhov, A.M.2    Klemm, R.D.3    Griffith, J.D.4    Bell, S.P.5
  • 42
    • 0034687677 scopus 로고    scopus 로고
    • Stepwise assembly of initiation proteins at budding yeast replication origins in vitro
    • Seki T., Diffley J.F. Stepwise assembly of initiation proteins at budding yeast replication origins in vitro. Proc Natl Acad Sci U S A 2000, 97:14115-14120.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14115-14120
    • Seki, T.1    Diffley, J.F.2
  • 43
    • 29544435484 scopus 로고    scopus 로고
    • Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase
    • Randell J.C., Bowers J.L., Rodriguez H.K., Bell S.P. Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase. Mol Cell 2006, 21:29-39.
    • (2006) Mol Cell , vol.21 , pp. 29-39
    • Randell, J.C.1    Bowers, J.L.2    Rodriguez, H.K.3    Bell, S.P.4
  • 44
    • 0028179973 scopus 로고
    • Cdt1 is an essential target of the Cdc10/Sct1 transcription factor: requirement for DNA replication and inhibition of mitosis
    • Hofmann J.F., Beach D. cdt1 is an essential target of the Cdc10/Sct1 transcription factor: requirement for DNA replication and inhibition of mitosis. EMBO J 1994, 13:425-434.
    • (1994) EMBO J , vol.13 , pp. 425-434
    • Hofmann, J.F.1    Beach, D.2
  • 45
    • 0034611749 scopus 로고    scopus 로고
    • The Cdt1 protein is required to license DNA for replication in fission yeast
    • Nishitani H., Lygerou Z., Nishimoto T., Nurse P. The Cdt1 protein is required to license DNA for replication in fission yeast. Nature 2000, 404:625-628.
    • (2000) Nature , vol.404 , pp. 625-628
    • Nishitani, H.1    Lygerou, Z.2    Nishimoto, T.3    Nurse, P.4
  • 46
    • 0028098812 scopus 로고
    • Two steps in the assembly of complexes at yeast replication origins in vivo
    • Diffley J.F., Cocker J.H., Dowell S.J., Rowley A. Two steps in the assembly of complexes at yeast replication origins in vivo. Cell 1994, 78:303-316.
    • (1994) Cell , vol.78 , pp. 303-316
    • Diffley, J.F.1    Cocker, J.H.2    Dowell, S.J.3    Rowley, A.4
  • 47
    • 70350751416 scopus 로고    scopus 로고
    • Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing
    • Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F. Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing. Cell 2009, 139:719-730.
    • (2009) Cell , vol.139 , pp. 719-730
    • Remus, D.1    Beuron, F.2    Tolun, G.3    Griffith, J.D.4    Morris, E.P.5    Diffley, J.F.6
  • 48
    • 73949091058 scopus 로고    scopus 로고
    • A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication
    • Evrin C., Clarke P., Zech J., Lurz R., Sun J., Uhle S., Li H., Stillman B., Speck C. A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication. Proc Natl Acad Sci U S A 2009, 106:20240-20245.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20240-20245
    • Evrin, C.1    Clarke, P.2    Zech, J.3    Lurz, R.4    Sun, J.5    Uhle, S.6    Li, H.7    Stillman, B.8    Speck, C.9
  • 49
    • 61849173573 scopus 로고    scopus 로고
    • Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation
    • Francis L.I., Randell J.C., Takara T.J., Uchima L., Bell S.P. Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation. Genes Dev 2009, 23:643-654.
    • (2009) Genes Dev , vol.23 , pp. 643-654
    • Francis, L.I.1    Randell, J.C.2    Takara, T.J.3    Uchima, L.4    Bell, S.P.5
  • 50
    • 33749075373 scopus 로고    scopus 로고
    • Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression
    • Sheu Y.J., Stillman B. Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression. Mol Cell 2006, 24:101-113.
    • (2006) Mol Cell , vol.24 , pp. 101-113
    • Sheu, Y.J.1    Stillman, B.2
  • 51
    • 0038680253 scopus 로고    scopus 로고
    • Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo
    • Kanemaki M., Sanchez-Diaz A., Gambus A., Labib K. Functional proteomic identification of DNA replication proteins by induced proteolysis in vivo. Nature 2003, 423:720-724.
    • (2003) Nature , vol.423 , pp. 720-724
    • Kanemaki, M.1    Sanchez-Diaz, A.2    Gambus, A.3    Labib, K.4
  • 53
    • 0037847620 scopus 로고    scopus 로고
    • GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast
    • Takayama Y., Kamimura Y., Okawa M., Muramatsu S., Sugino A., Araki H. GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast. Genes Dev 2003, 17:1153-1165.
    • (2003) Genes Dev , vol.17 , pp. 1153-1165
    • Takayama, Y.1    Kamimura, Y.2    Okawa, M.3    Muramatsu, S.4    Sugino, A.5    Araki, H.6
  • 54
    • 33645717628 scopus 로고    scopus 로고
    • GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks
    • Gambus A. GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks. Nat Cell Biol 2006, 8:358-366.
    • (2006) Nat Cell Biol , vol.8 , pp. 358-366
    • Gambus, A.1
  • 55
    • 33745925880 scopus 로고    scopus 로고
    • Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase
    • Moyer S.E., Lewis P.W., Botchan M.R. Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A 2006, 103:10236-10241.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 10236-10241
    • Moyer, S.E.1    Lewis, P.W.2    Botchan, M.R.3
  • 59
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control
    • Liu J., Smith C.L., DeRyckere D., DeAngelis K., Martin G.S., Berger J.M. Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol Cell 2000, 6:637-648.
    • (2000) Mol Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    DeRyckere, D.3    DeAngelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 60
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
    • Erzberger J.P., Pirruccello M.M., Berger J.M. The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J 2002, 21:4763-4773.
    • (2002) EMBO J , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 61
    • 4744353204 scopus 로고    scopus 로고
    • Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix
    • Singleton M.R., Morales R., Grainge I., Cook N., Isupov M.N., Wigley D.B. Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix. J Mol Biol 2004, 343:547-557.
    • (2004) J Mol Biol , vol.343 , pp. 547-557
    • Singleton, M.R.1    Morales, R.2    Grainge, I.3    Cook, N.4    Isupov, M.N.5    Wigley, D.B.6
  • 62
    • 34548530410 scopus 로고    scopus 로고
    • Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex
    • Dueber E.L., Corn J.E., Bell S.D., Berger J.M. Replication origin recognition and deformation by a heterodimeric archaeal Orc1 complex. Science (New York, NY) 2007, 317:1210-1213.
    • (2007) Science (New York, NY) , vol.317 , pp. 1210-1213
    • Dueber, E.L.1    Corn, J.E.2    Bell, S.D.3    Berger, J.M.4
  • 64
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Erzberger J.P., Mott M.L., Berger J.M. Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat Struct Mol Biol 2006, 13:676-683.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 65
    • 84858794276 scopus 로고    scopus 로고
    • Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA
    • Scholefield G., Errington J., Murray H. Soj/ParA stalls DNA replication by inhibiting helix formation of the initiator protein DnaA. EMBO J 2012, 31:1542-1555.
    • (2012) EMBO J , vol.31 , pp. 1542-1555
    • Scholefield, G.1    Errington, J.2    Murray, H.3
  • 66
    • 77956259937 scopus 로고    scopus 로고
    • Origin remodeling and opening in bacteria rely on distinct assembly states of the DnaA initiator
    • Duderstadt K.E., Mott M.L., Crisona N.J., Chuang K., Yang H., Berger J.M. Origin remodeling and opening in bacteria rely on distinct assembly states of the DnaA initiator. J Biol Chem 2010, 285:28229-28239.
    • (2010) J Biol Chem , vol.285 , pp. 28229-28239
    • Duderstadt, K.E.1    Mott, M.L.2    Crisona, N.J.3    Chuang, K.4    Yang, H.5    Berger, J.M.6
  • 67
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: common structure-diverse function
    • Ogura T., Wilkinson A.J. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells: Mol Cell Mech 2001, 6:575-597.
    • (2001) Genes Cells: Mol Cell Mech , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 69
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • 489-484
    • Chen Z., Yang H., Pavletich N.P. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 2008, 453. 489-484.
    • (2008) Nature , vol.453
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 70
    • 33847778234 scopus 로고    scopus 로고
    • Motoring along with the bacterial RecA protein
    • Cox M.M. Motoring along with the bacterial RecA protein. Nat Rev Mol Cell Biol 2007, 8:127-138.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 127-138
    • Cox, M.M.1
  • 71
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark E.J., Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 2006, 442:270-275.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 73
    • 0033485526 scopus 로고    scopus 로고
    • Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli
    • Kurokawa K., Nishida S., Emoto A., Sekimizu K., Katayama T. Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli. EMBO J 1999, 18:6642-6652.
    • (1999) EMBO J , vol.18 , pp. 6642-6652
    • Kurokawa, K.1    Nishida, S.2    Emoto, A.3    Sekimizu, K.4    Katayama, T.5
  • 74
    • 0032504050 scopus 로고    scopus 로고
    • The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase
    • Katayama T., Kubota T., Kurokawa K., Crooke E., Sekimizu K. The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase. Cell 1998, 94:61-71.
    • (1998) Cell , vol.94 , pp. 61-71
    • Katayama, T.1    Kubota, T.2    Kurokawa, K.3    Crooke, E.4    Sekimizu, K.5
  • 75
    • 74749095240 scopus 로고    scopus 로고
    • Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins
    • Ilves I., Petojevic T., Pesavento J.J., Botchan M.R. Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins. Mol Cell 2010, 37:247-258.
    • (2010) Mol Cell , vol.37 , pp. 247-258
    • Ilves, I.1    Petojevic, T.2    Pesavento, J.J.3    Botchan, M.R.4
  • 77
    • 70549085855 scopus 로고    scopus 로고
    • Eukaryotic DNA replication control: lock and load, then fire
    • Remus D., Diffley J.F. Eukaryotic DNA replication control: lock and load, then fire. Curr Opin Cell Biol 2009, 21:771-777.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 771-777
    • Remus, D.1    Diffley, J.F.2
  • 79
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe D.D., Koonin E.V., Aravind L. Evolution and classification of P-loop kinases and related proteins. J Mol Biol 2003, 333:781-815.
    • (2003) J Mol Biol , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 81
    • 33646754407 scopus 로고    scopus 로고
    • Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert
    • Jenkinson E.R., Chong J.P. Minichromosome maintenance helicase activity is controlled by N- and C-terminal motifs and requires the ATPase domain helix-2 insert. Proc Natl Acad Sci U S A 2006, 103:7613-7618.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7613-7618
    • Jenkinson, E.R.1    Chong, J.P.2
  • 82
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • McGeoch A.T., Trakselis M.A., Laskey R.A., Bell S.D. Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism. Nat Struct Mol Biol 2005, 12:756-762.
    • (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
  • 83
    • 0034655949 scopus 로고    scopus 로고
    • The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework
    • Krebs W.G., Gerstein M. The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework. Nucleic Acids Res 2000, 28:1665-1675.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.