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Volumn 287, Issue 44, 2012, Pages 37458-37471

Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOMAL REPLICATION; DNA UNWINDING; REPLICATION INITIATION; STRUCTURAL MOTIFS;

EID: 84868252479     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.372052     Document Type: Article
Times cited : (47)

References (70)
  • 1
    • 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., and Kornberg, A. (1988) Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell 52, 743-755
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 2
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiateDNAreplication
    • Messer, W. (2002) The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiateDNAreplication. FEMS Microbiol. Rev. 26, 355-374
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 355-374
    • Messer, W.1
  • 4
    • 67650717209 scopus 로고    scopus 로고
    • DnaA structure, function, and dynamics in the initiation at the chromosomal origin
    • Ozaki, S., and Katayama, T. (2009) DnaA structure, function, and dynamics in the initiation at the chromosomal origin. Plasmid 62, 71-82
    • (2009) Plasmid , vol.62 , pp. 71-82
    • Ozaki, S.1    Katayama, T.2
  • 5
    • 78649670055 scopus 로고    scopus 로고
    • Regulating DnaA complex assembly. It is time to fill the gaps
    • Leonard, A. C., and Grimwade, J. E. (2010) Regulating DnaA complex assembly. It is time to fill the gaps. Curr. Opin. Microbiol. 13, 766-772
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 766-772
    • Leonard, A.C.1    Grimwade, J.E.2
  • 6
    • 80053564711 scopus 로고    scopus 로고
    • Replication initiation at the Escherichia coli chromosomal origin
    • Kaguni, J. M. (2011) Replication initiation at the Escherichia coli chromosomal origin. Curr. Opin. Chem. Biol. 15, 606-613
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 606-613
    • Kaguni, J.M.1
  • 7
    • 73649145533 scopus 로고    scopus 로고
    • Primase directs the release of DnaC from DnaB
    • Makowska-Grzyska, M., and Kaguni, J. M. (2010) Primase directs the release of DnaC from DnaB. Mol. Cell 37, 90-101
    • (2010) Mol. Cell , vol.37 , pp. 90-101
    • Makowska-Grzyska, M.1    Kaguni, J.M.2
  • 8
    • 84858860484 scopus 로고    scopus 로고
    • Loading mechanisms of ring helicases at replication origins
    • Soultanas, P. (2012) Loading mechanisms of ring helicases at replication origins. Mol. Microbiol. 84, 6-16
    • (2012) Mol. Microbiol. , vol.84 , pp. 6-16
    • Soultanas, P.1
  • 9
    • 33749033347 scopus 로고    scopus 로고
    • The replication clamp-loading machine at work in the three domains of life
    • Indiani, C., and O'Donnell, M. (2006) The replication clamp-loading machine at work in the three domains of life. Nat. Rev. Mol. Cell Biol. 7, 751-761
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 751-761
    • Indiani, C.1    O'donnell, M.2
  • 10
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller, R. C., and Marians, K. J. (2006) Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7, 932-943
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 11
    • 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., and Sekimizu, K. (1998) The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase. Cell 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
  • 12
    • 61349152435 scopus 로고    scopus 로고
    • Hda monomerization by ADP binding promotes replicase clampmediated DnaA-ATP hydrolysis
    • Su'etsugu, M., Nakamura, K., Keyamura, K., Kudo, Y., and Katayama, T. (2008) Hda monomerization by ADP binding promotes replicase clampmediated DnaA-ATP hydrolysis. J. Biol. Chem. 283, 36118-36131
    • (2008) J. Biol. Chem. , vol.283 , pp. 36118-36131
    • Su'etsugu, M.1    Nakamura, K.2    Keyamura, K.3    Kudo, Y.4    Katayama, T.5
  • 13
    • 77951150088 scopus 로고    scopus 로고
    • Novel essential residues of Hda for interaction with DnaA in the regulatory inactivation of DnaA. Unique roles for Hda AAA Box VI and VII motifs
    • Nakamura, K., and Katayama, T. (2010) Novel essential residues of Hda for interaction with DnaA in the regulatory inactivation of DnaA. Unique roles for Hda AAA Box VI and VII motifs. Mol. Microbiol. 76, 302-317
    • (2010) Mol. Microbiol. , vol.76 , pp. 302-317
    • Nakamura, K.1    Katayama, T.2
  • 14
    • 80051686887 scopus 로고    scopus 로고
    • DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA
    • Keyamura, K., and Katayama, T. (2011) DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA. J. Biol. Chem. 286, 29336-29346
    • (2011) J. Biol. Chem. , vol.286 , pp. 29336-29346
    • Keyamura, K.1    Katayama, T.2
  • 15
    • 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., and Fujimitsu, K. (2010) Regulation of the replication cycle. Conserved and diverse regulatory systems for DnaA and oriC. Nat. Rev. Microbiol. 8, 163-170
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 163-170
    • Katayama, T.1    Ozaki, S.2    Keyamura, K.3    Fujimitsu, K.4
  • 16
    • 0023658349 scopus 로고
    • ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu, K., Bramhill, D., and Kornberg, A. (1987) ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell 50, 259-265
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 17
    • 48149106768 scopus 로고    scopus 로고
    • Modes of overinitiation, dnaA gene expression, and inhibition of cell division in a novel cold-sensitive hda mutant of Escherichia coli
    • Fujimitsu, K., Su'etsugu, M., Yamaguchi, Y., Mazda, K., Fu, N., Kawakami, H., and Katayama, T. (2008) Modes of overinitiation, dnaA gene expression, and inhibition of cell division in a novel cold-sensitive hda mutant of Escherichia coli. J. Bacteriol. 190, 5368-5381
    • (2008) J. Bacteriol. , vol.190 , pp. 5368-5381
    • Fujimitsu, K.1    Su'etsugu, M.2    Yamaguchi, Y.3    Mazda, K.4    Fu, N.5    Kawakami, H.6    Katayama, T.7
  • 18
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • Kato, J., and Katayama, T. (2001) Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli. EMBO J. 20, 4253-4262
    • (2001) EMBO J. , vol.20 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 19
    • 29744460566 scopus 로고    scopus 로고
    • Hda inactivation of DnaA is the predominant mechanism preventing hyperinitiation of Escherichia coli DNA replication
    • Camara, J. E., Breier, A. M., Brendler, T., Austin, S., Cozzarelli, N. R., and Crooke, E. (2005) Hda inactivation of DnaA is the predominant mechanism preventing hyperinitiation of Escherichia coli DNA replication. EMBO Rep. 6, 736-741
    • (2005) EMBO Rep. , vol.6 , pp. 736-741
    • Camara, J.E.1    Breier, A.M.2    Brendler, T.3    Austin, S.4    Cozzarelli, N.R.5    Crooke, E.6
  • 20
    • 33644861714 scopus 로고    scopus 로고
    • A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli
    • Gon, S., Camara, J. E., Klungsøyr, H. K., Crooke, E., Skarstad, K., and Beckwith, J. (2006) A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli. EMBO J. 25, 1137-1147
    • (2006) EMBO J. , vol.25 , pp. 1137-1147
    • Gon, S.1    Camara, J.E.2    Klungsøyr, H.K.3    Crooke, E.4    Skarstad, K.5    Beckwith, J.6
  • 21
    • 58149123595 scopus 로고    scopus 로고
    • Loss of Hda activity stimulates replication initiation from I-box but not R4 mutant origins in Escherichia coli
    • Riber, L., Fujimitsu, K., Katayama, T., and Løbner-Olesen, A. (2009) Loss of Hda activity stimulates replication initiation from I-box but not R4 mutant origins in Escherichia coli. Mol. Microbiol. 71, 107-122
    • (2009) Mol. Microbiol. , vol.71 , pp. 107-122
    • Riber, L.1    Fujimitsu, K.2    Katayama, T.3    Løbner-Olesen, A.4
  • 23
    • 66149097454 scopus 로고    scopus 로고
    • Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA
    • Fujimitsu, K., Senriuchi, T., and Katayama, T. (2009) Specific genomic sequences of E. coli promote replicational initiation by directly reactivating ADP-DnaA. Genes Dev. 23, 1221-1233
    • (2009) Genes Dev. , vol.23 , pp. 1221-1233
    • Fujimitsu, K.1    Senriuchi, T.2    Katayama, T.3
  • 24
    • 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., and Katayama, T. (2005) Formation of an ATP-DnaA-specific initiation complex requires DnaA arginine 285, a conserved motif in the AAA+ protein family. J. Biol. Chem. 280, 27420-27430
    • (2005) J. Biol. Chem. , vol.280 , pp. 27420-27430
    • Kawakami, H.1    Keyamura, K.2    Katayama, T.3
  • 25
    • 1542297764 scopus 로고    scopus 로고
    • Two discriminatory binding sites in the Escherichia coli replication origin are required for DNA strand opening by initiator DnaA-ATP
    • McGarry, K. C., Ryan, V. T., Grimwade, J. E., and Leonard, A. C. (2004) Two discriminatory binding sites in the Escherichia coli replication origin are required for DNA strand opening by initiator DnaA-ATP. Proc. Natl. Acad. Sci. U.S.A. 101, 2811-2816
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2811-2816
    • McGarry, K.C.1    Ryan, V.T.2    Grimwade, J.E.3    Leonard, A.C.4
  • 26
    • 80053969192 scopus 로고    scopus 로고
    • Two oppositely oriented arrays of low affinity recognition sites in oriC guide progressive binding of DnaA during Escherichia coli pre-RC assembly
    • Rozgaja, T. A., Grimwade, J. E., Iqbal, M., Czerwonka, C., Vora, M., and Leonard, A. C. (2011) Two oppositely oriented arrays of low affinity recognition sites in oriC guide progressive binding of DnaA during Escherichia coli pre-RC assembly. Mol. Microbiol. 82, 475-488
    • (2011) Mol. Microbiol. , vol.82 , pp. 475-488
    • Rozgaja, T.A.1    Grimwade, J.E.2    Iqbal, M.3    Czerwonka, C.4    Vora, M.5    Leonard, A.C.6
  • 27
    • 0029088758 scopus 로고
    • Interaction of the initiator protein DnaA of Escherichia coli with its DNA target
    • Schaper, S., and Messer, W. (1995) Interaction of the initiator protein DnaA of Escherichia coli with its DNA target. J. Biol. Chem. 270, 17622-17626
    • (1995) J. Biol. Chem. , vol.270 , pp. 17622-17626
    • Schaper, S.1    Messer, W.2
  • 30
    • 0025058738 scopus 로고
    • Fate of the DnaA initiator protein in replication at the origin of the Escherichia coli chromosome in vitro
    • Yung, B. Y., Crooke, E., and Kornberg, A. (1990) Fate of the DnaA initiator protein in replication at the origin of the Escherichia coli chromosome in vitro. J. Biol. Chem. 265, 1282-1285
    • (1990) J. Biol. Chem. , vol.265 , pp. 1282-1285
    • Yung, B.Y.1    Crooke, E.2    Kornberg, A.3
  • 31
    • 84857873014 scopus 로고    scopus 로고
    • Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation
    • Ozaki, S., and Katayama, T. (2012) Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation. Nucleic Acids Res. 40, 1648-1665
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1648-1665
    • Ozaki, S.1    Katayama, T.2
  • 32
    • 0036436076 scopus 로고    scopus 로고
    • Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC
    • Weigel, C., and Seitz, H. (2002) Strand-specific loading of DnaB helicase by DnaA to a substrate mimicking unwound oriC. Mol. Microbiol. 46, 1149-1156
    • (2002) Mol. Microbiol. , vol.46 , pp. 1149-1156
    • Weigel, C.1    Seitz, H.2
  • 33
    • 76949089832 scopus 로고    scopus 로고
    • Bacterial nucleoid-associated proteins, nucleoid structure and gene expression
    • Dillon, S. C., and Dorman, C. J. (2010) Bacterial nucleoid-associated proteins, nucleoid structure and gene expression. Nat. Rev. Microbiol. 8, 185-195
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 185-195
    • Dillon, S.C.1    Dorman, C.J.2
  • 34
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang, D. S., and Kornberg, A. (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J. Biol. Chem. 267, 23083-23086
    • (1992) J. Biol. Chem. , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 35
    • 0036035581 scopus 로고    scopus 로고
    • IHF and HUstimulate assembly of prereplication complexes at Escherichia coli oriC by two different mechanisms
    • Ryan, V. T., Grimwade, J. E., Nievera, C. J., and Leonard, A. C. (2002) IHF andHUstimulate assembly of prereplication complexes at Escherichia coli oriC by two different mechanisms. Mol. Microbiol. 46, 113-124
    • (2002) Mol. Microbiol. , vol.46 , pp. 113-124
    • Ryan, V.T.1    Grimwade, J.E.2    Nievera, C.J.3    Leonard, A.C.4
  • 36
    • 0035038813 scopus 로고    scopus 로고
    • The sequence requirements for a functional Escherichia coli replication origin are different for the chromosome and a minichromosome
    • Weigel, C., Messer, W., Preiss, S., Welzeck, M., Morigen, and Boye, E. (2001) The sequence requirements for a functional Escherichia coli replication origin are different for the chromosome and a minichromosome. Mol. Microbiol. 40, 498-507
    • (2001) Mol. Microbiol. , vol.40 , pp. 498-507
    • Weigel, C.1    Messer, W.2    Preiss, S.3    Morigen, W.M.4    Boye, E.5
  • 37
    • 14544286823 scopus 로고    scopus 로고
    • Building a bacterial orisome. Emergence of new regulatory features for replication origin unwinding
    • Leonard, A. C., and Grimwade, J. E. (2005) Building a bacterial orisome. Emergence of new regulatory features for replication origin unwinding. Mol. Microbiol. 55, 978-985
    • (2005) Mol. Microbiol. , vol.55 , pp. 978-985
    • Leonard, A.C.1    Grimwade, J.E.2
  • 38
    • 0035869023 scopus 로고    scopus 로고
    • Mechanism of origin unwinding. Sequential binding of DnaA to double- and single-stranded DNA
    • Speck, C., and Messer, W. (2001) Mechanism of origin unwinding. Sequential binding of DnaA to double- and single-stranded DNA. EMBO J. 20, 1469-1476
    • (2001) EMBO J. , vol.20 , pp. 1469-1476
    • Speck, C.1    Messer, W.2
  • 39
    • 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., and Berger, J. M. (2010) Origin remodeling and opening in bacteria rely on distinct assembly states of the DnaA initiator. J. Biol. Chem. 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
  • 40
    • 80054029342 scopus 로고    scopus 로고
    • DNA stretching by bacterial initiators promotes replication origin opening
    • Duderstadt, K. E., Chuang, K., and Berger, J. M. (2011) DNA stretching by bacterial initiators promotes replication origin opening. Nature 478, 209-213
    • (2011) Nature , vol.478 , pp. 209-213
    • Duderstadt, K.E.1    Chuang, K.2    Berger, J.M.3
  • 41
    • 21644437635 scopus 로고    scopus 로고
    • An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin
    • Felczak, M. M., Simmons, L. A., and Kaguni, J. M. (2005) An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin. J. Biol. Chem. 280, 24627-24633
    • (2005) J. Biol. Chem. , vol.280 , pp. 24627-24633
    • Felczak, M.M.1    Simmons, L.A.2    Kaguni, J.M.3
  • 42
    • 69949170409 scopus 로고    scopus 로고
    • DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading
    • Keyamura, K., Abe, Y., Higashi, M., Ueda, T., and Katayama, T. (2009) DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading. J. Biol. Chem. 284, 25038-25050
    • (2009) J. Biol. Chem. , vol.284 , pp. 25038-25050
    • Keyamura, K.1    Abe, Y.2    Higashi, M.3    Ueda, T.4    Katayama, T.5
  • 43
    • 34547100313 scopus 로고    scopus 로고
    • Structure and function of DnaA N-terminal domains. Specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC
    • Abe, Y., Jo, T., Matsuda, Y., Matsunaga, C., Katayama, T., and Ueda, T. (2007) Structure and function of DnaA N-terminal domains. Specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC. J. Biol. Chem. 282, 17816-17827
    • (2007) J. Biol. Chem. , vol.282 , pp. 17816-17827
    • Abe, Y.1    Jo, T.2    Matsuda, Y.3    Matsunaga, C.4    Katayama, T.5    Ueda, T.6
  • 44
    • 57349172060 scopus 로고    scopus 로고
    • Determination of the minimum domain II size of Escherichia coli DnaA protein essential for cell viability
    • Nozaki, S., and Ogawa, T. (2008) Determination of the minimum domain II size of Escherichia coli DnaA protein essential for cell viability. Microbiology 154, 3379-3384
    • (2008) Microbiology , vol.154 , pp. 3379-3384
    • Nozaki, S.1    Ogawa, T.2
  • 45
    • 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., and Koonin, E. V. (1999) AAA+. A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 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
  • 46
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA. Implications for general mechanisms underlying DNA replication initiation
    • Erzberger, J. P., Pirruccello, M. M., and Berger, J. M. (2002) The structure of bacterial DnaA. Implications for general mechanisms underlying DNA replication initiation. EMBO J. 21, 4763-4773
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 48
    • 80053205982 scopus 로고    scopus 로고
    • Remodeling of nucleoprotein complexes is independent of the nucleotide state of a mutant AAA+ protein
    • Saxena, R., Rozgaja, T., Grimwade, J., and Crooke, E. (2011) Remodeling of nucleoprotein complexes is independent of the nucleotide state of a mutant AAA+ protein. J. Biol. Chem. 286, 33770-33777
    • (2011) J. Biol. Chem. , vol.286 , pp. 33770-33777
    • Saxena, R.1    Rozgaja, T.2    Grimwade, J.3    Crooke, E.4
  • 49
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication origin remodeling
    • Erzberger, J. P., Mott, M. L., and Berger, J. M. (2006) Structural basis for ATP-dependent DnaA assembly and replication origin remodeling. Nat. Struct. Mol. Biol. 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
  • 50
    • 33645133194 scopus 로고    scopus 로고
    • The DnaA homolog of the hyperthermophilic eubacterium Thermotoga maritima forms an open complex with a minimal 149-bp origin region in an ATP-dependent manner
    • Ozaki, S., Fujimitsu, K., Kurumizaka, H., and Katayama, T. (2006) The DnaA homolog of the hyperthermophilic eubacterium Thermotoga maritima forms an open complex with a minimal 149-bp origin region in an ATP-dependent manner. Genes Cells 11, 425-438
    • (2006) Genes Cells , vol.11 , pp. 425-438
    • Ozaki, S.1    Fujimitsu, K.2    Kurumizaka, H.3    Katayama, T.4
  • 51
    • 33750742434 scopus 로고    scopus 로고
    • The exceptionally tight affinity of DnaA for ATP/ADP requires a unique aspartic acid residue in the AAA+ sensor 1 motif
    • Kawakami, H., Ozaki, S., Suzuki, S., Nakamura, K., Senriuchi, T., Su'etsugu, M., Fujimitsu, K., and Katayama, T. (2006) The exceptionally tight affinity of DnaA for ATP/ADP requires a unique aspartic acid residue in the AAA+ sensor 1 motif. Mol. Microbiol. 62, 1310-1324
    • (2006) Mol. Microbiol. , vol.62 , pp. 1310-1324
    • Kawakami, H.1    Ozaki, S.2    Suzuki, S.3    Nakamura, K.4    Senriuchi, T.5    Su'etsugu, M.6    Fujimitsu, K.7    Katayama, T.8
  • 52
    • 0030737725 scopus 로고    scopus 로고
    • Stable DNA replication. Interplay between DNA replication, homologous recombination, and transcription
    • Kogoma, T. (1997) Stable DNA replication. Interplay between DNA replication, homologous recombination, and transcription. Microbiol. Mol. Biol. Rev. 61, 212-238
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 212-238
    • Kogoma, T.1
  • 53
    • 70349904184 scopus 로고    scopus 로고
    • The right half of the Escherichia coli replication origin is not essential for viability but facilitates multiforked replication
    • Stepankiw, N., Kaidow, A., Boye, E., and Bates, D. (2009) The right half of the Escherichia coli replication origin is not essential for viability but facilitates multiforked replication. Mol. Microbiol. 74, 467-479
    • (2009) Mol. Microbiol. , vol.74 , pp. 467-479
    • Stepankiw, N.1    Kaidow, A.2    Boye, E.3    Bates, D.4
  • 54
    • 0032545466 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin
    • Sutton, M. D., Carr, K. M., Vicente, M., and Kaguni, J. M. (1998) Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin. J. Biol. Chem. 273, 34255-34262
    • (1998) J. Biol. Chem. , vol.273 , pp. 34255-34262
    • Sutton, M.D.1    Carr, K.M.2    Vicente, M.3    Kaguni, J.M.4
  • 55
    • 0028867701 scopus 로고
    • Cell cyclespecific changes in nucleoprotein complexes at a chromosomal replication origin
    • Cassler, M. R., Grimwade, J. E., and Leonard, A. C. (1995) Cell cyclespecific changes in nucleoprotein complexes at a chromosomal replication origin. EMBO J. 14, 5833-5841
    • (1995) EMBO J. , vol.14 , pp. 5833-5841
    • Cassler, M.R.1    Grimwade, J.E.2    Leonard, A.C.3
  • 56
    • 33750987654 scopus 로고    scopus 로고
    • SeqA blocking of DnaA-oriC interactions ensures staged assembly of the E. coli pre-RC
    • Nievera, C., Torgue, J. J., Grimwade, J. E., and Leonard, A. C. (2006) SeqA blocking of DnaA-oriC interactions ensures staged assembly of the E. coli pre-RC. Mol. Cell 24, 581-592
    • (2006) Mol. Cell , vol.24 , pp. 581-592
    • Nievera, C.1    Torgue, J.J.2    Grimwade, J.E.3    Leonard, A.C.4
  • 57
    • 0024462061 scopus 로고
    • In vivo studies of DnaA binding to the origin of replication of Escherichia coli
    • Samitt, C. E., Hansen, F. G., Miller, J. F., and Schaechter, M. (1989) In vivo studies of DnaA binding to the origin of replication of Escherichia coli. EMBO J. 8, 989-993
    • (1989) EMBO J. , vol.8 , pp. 989-993
    • Samitt, C.E.1    Hansen, F.G.2    Miller, J.F.3    Schaechter, M.4
  • 58
    • 0033485526 scopus 로고    scopus 로고
    • Replication cycle-coordinated change of the adenine nucleotidebound forms of DnaA protein in Escherichia coli
    • Kurokawa, K., Nishida, S., Emoto, A., Sekimizu, K., and Katayama, T. (1999) Replication cycle-coordinated change of the adenine nucleotidebound forms of DnaA protein in Escherichia coli. EMBO J. 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
  • 59
    • 0037177830 scopus 로고    scopus 로고
    • A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication. Evidnece from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo
    • Nishida, S., Fujimitsu, K., Sekimizu, K., Ohmura, T., Ueda, T., and Katayama, T. (2002) A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication. Evidnece from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo. J. Biol. Chem. 277, 14986-14995
    • (2002) J. Biol. Chem. , vol.277 , pp. 14986-14995
    • Nishida, S.1    Fujimitsu, K.2    Sekimizu, K.3    Ohmura, T.4    Ueda, T.5    Katayama, T.6
  • 60
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases. ATP-fueled machines of protein destruction
    • Sauer, R. T., and Baker, T. A. (2011) AAA+ proteases. ATP-fueled machines of protein destruction. Annu. Rev. Biochem. 80, 587-612
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 61
    • 70350772363 scopus 로고    scopus 로고
    • Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in an AAA+ protein-unfolding machine
    • Glynn, S. E., Martin, A., Nager, A. R., Baker, T. A., and Sauer, R. T. (2009) Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in an AAA+ protein-unfolding machine. Cell 139, 744-756
    • (2009) Cell , vol.139 , pp. 744-756
    • Glynn, S.E.1    Martin, A.2    Nager, A.R.3    Baker, T.A.4    Sauer, R.T.5
  • 62
    • 84855198122 scopus 로고    scopus 로고
    • Structure and function of the bacterial AAA protease FtsH
    • Langklotz, S., Baumann, U., and Narberhaus, F. (2012) Structure and function of the bacterial AAA protease FtsH. Biochim. Biophys. Acta 1823, 40-48
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 40-48
    • Langklotz, S.1    Baumann, U.2    Narberhaus, F.3
  • 63
    • 55549088522 scopus 로고    scopus 로고
    • Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
    • Martin, A., Baker, T. A., and Sauer, R. T. (2008) Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding. Nat. Struct. Mol. Biol. 15, 1147-1151
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1147-1151
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 64
    • 79953888421 scopus 로고    scopus 로고
    • Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
    • Aubin-Tam, M. E., Olivares, A. O., Sauer, R. T., Baker, T. A., and Lang, M. J. (2011) Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell 145, 257-267
    • (2011) Cell , vol.145 , pp. 257-267
    • Aubin-Tam, M.E.1    Olivares, A.O.2    Sauer, R.T.3    Baker, T.A.4    Lang, M.J.5
  • 65
    • 79951707743 scopus 로고    scopus 로고
    • ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle
    • Smith, D. M., Fraga, H., Reis, C., Kafri, G., and Goldberg, A. L. (2011) ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144, 526-538
    • (2011) Cell , vol.144 , pp. 526-538
    • Smith, D.M.1    Fraga, H.2    Reis, C.3    Kafri, G.4    Goldberg, A.L.5
  • 66
    • 0030035666 scopus 로고    scopus 로고
    • Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli
    • Margulies, C., and Kaguni, J. M. (1996) Ordered and sequential binding of DnaA protein to oriC, the chromosomal origin of Escherichia coli. J. Biol. Chem. 271, 17035-17040
    • (1996) J. Biol. Chem. , vol.271 , pp. 17035-17040
    • Margulies, C.1    Kaguni, J.M.2
  • 67
    • 81055138204 scopus 로고    scopus 로고
    • Quality control in the initiation of eukaryotic DNA replication
    • Diffley, J. F. (2011) Quality control in the initiation of eukaryotic DNA replication. Philos. Trans. R. Soc. Lond. B Biol. Sci. 366, 3545-3553
    • (2011) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.366 , pp. 3545-3553
    • Diffley, J.F.1
  • 68
    • 14544277626 scopus 로고    scopus 로고
    • Origin recognition and the chromosome cycle
    • Stillman, B. (2005) Origin recognition and the chromosome cycle. FEBS Lett. 579, 877-884
    • (2005) FEBS Lett. , vol.579 , pp. 877-884
    • Stillman, B.1
  • 69
    • 75349083245 scopus 로고    scopus 로고
    • DnaA, ORC, and Cdc6. Similarity beyond the domains of life and diversity
    • Kawakami, H., and Katayama, T. (2010) DnaA, ORC, and Cdc6. Similarity beyond the domains of life and diversity. Biochem. Cell Biol. 88, 49-62
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 49-62
    • Kawakami, H.1    Katayama, T.2


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