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Volumn 62, Issue 5, 2006, Pages 1310-1324

The exceptionally tight affinity of DnaA for ATP/ADP requires a unique aspartic acid residue in the AAA+ sensor 1 motif

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE; ASPARTIC ACID; BACTERIAL PROTEIN; PROTEIN; PROTEIN DNAA; PROTEIN DNAB; THREONINE; UNCLASSIFIED DRUG;

EID: 33750742434     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05450.x     Document Type: Article
Times cited : (33)

References (59)
  • 2
    • 0023152226 scopus 로고
    • Overproduction of DnaA protein stimulates initiation of chromosome and minichromosome replication in Escherichia coli
    • Atlung, T., Løbner-Olesen, A., and Hansen, F.G. (1987) Overproduction of DnaA protein stimulates initiation of chromosome and minichromosome replication in Escherichia coli. Mol Gen Genet 206: 51-59.
    • (1987) Mol Gen Genet , vol.206 , pp. 51-59
    • Atlung, T.1    Løbner-Olesen, A.2    Hansen, F.G.3
  • 3
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman, G.D., O'Donnell, M., and Kuriyan, J. (2004) Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429: 724-730.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 4
    • 0037131160 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin
    • Carr, K.M., and Kaguni, J.M. (2002) Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin. J Biol Chem 277: 39815-39822.
    • (2002) J Biol Chem , vol.277 , pp. 39815-39822
    • Carr, K.M.1    Kaguni, J.M.2
  • 5
    • 0037124375 scopus 로고    scopus 로고
    • The DnaC helicase loader is a dual ATP/ADP switch protein
    • Davey, M.J., Fang, L., McInerney, P., Georgescu, R.E., and O'Donnell, M. (2002) The DnaC helicase loader is a dual ATP/ADP switch protein. EMBO J 21: 3148-3159.
    • (2002) EMBO J , vol.21 , pp. 3148-3159
    • Davey, M.J.1    Fang, L.2    McInerney, P.3    Georgescu, R.E.4    O'Donnell, M.5
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • Fenn, T.D., Ringea, D., and Petsko, G.A. (2003) POVScript+: a program for model and data visualization using persistence of vision ray-tracing. J Appl Crystallogr 36: 944-947.
    • (2003) J Appl Crystallogr , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringea, D.2    Petsko, G.A.3
  • 10
    • 0029880647 scopus 로고    scopus 로고
    • Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein
    • Garner, J., and Crooke, E. (1996) Membrane regulation of the chromosomal replication activity of E. coli DnaA requires a discrete site on the protein. EMBO J 15: 3477-3485.
    • (1996) EMBO J , vol.15 , pp. 3477-3485
    • Garner, J.1    Crooke, E.2
  • 11
    • 30044443816 scopus 로고    scopus 로고
    • VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase
    • Gerega, A., Rockel, B., Peters, J., Tamura, T., Baumeister, W., and Zwickl, P. (2005) VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase. J Biol Chem 280: 42856-42862.
    • (2005) J Biol Chem , vol.280 , pp. 42856-42862
    • Gerega, A.1    Rockel, B.2    Peters, J.3    Tamura, T.4    Baumeister, W.5    Zwickl, P.6
  • 12
    • 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
  • 14
    • 0037080611 scopus 로고    scopus 로고
    • Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
    • Hattendorf, D.A., and Lindquist, S.L. (2002) Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J 21: 12-21.
    • (2002) EMBO J , vol.21 , pp. 12-21
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 15
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • Higuchi, K., Katayama, T., Iwai, S., Hidaka, M., Horiuchi, T., and Maki, H. (2003) Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro. Genes Cells 8: 437-449.
    • (2003) Genes Cells , vol.8 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 16
    • 0027518125 scopus 로고
    • Activation of DnaA5 protein by GrpE and DnaK heat shock proteins in initiation of DNA replication in Escherichia coli
    • Hupp, T.R., and Kaguni, J.M. (1993) Activation of DnaA5 protein by GrpE and DnaK heat shock proteins in initiation of DNA replication in Escherichia coli. J Biol Chem 268: 13137-13142.
    • (1993) J Biol Chem , vol.268 , pp. 13137-13142
    • Hupp, T.R.1    Kaguni, J.M.2
  • 17
    • 0025821264 scopus 로고
    • dnaK protein stimulates a mutant form of dnaA protein in Escherichia coli DNA replication
    • Hwang, D.S., and Kaguni, J.M. (1991) dnaK protein stimulates a mutant form of dnaA protein in Escherichia coli DNA replication. J Biol Chem 266: 7537-7541.
    • (1991) J Biol Chem , vol.266 , pp. 7537-7541
    • Hwang, D.S.1    Kaguni, J.M.2
  • 18
    • 0041706282 scopus 로고    scopus 로고
    • Inhibitory effects of basic or neutral phospholipid on acidic phospholipid-mediated dissociation of adenine nucleotide bound to DnaA protein, the initiator of chromosomal DNA replication
    • Ichihashi, N., Kurokawa, K., Matsuo, M., Kaito, C., and Sekimizu, K. (2003) Inhibitory effects of basic or neutral phospholipid on acidic phospholipid-mediated dissociation of adenine nucleotide bound to DnaA protein, the initiator of chromosomal DNA replication. J Biol Chem 278: 28778-28786.
    • (2003) J Biol Chem , vol.278 , pp. 28778-28786
    • Ichihashi, N.1    Kurokawa, K.2    Matsuo, M.3    Kaito, C.4    Sekimizu, K.5
  • 19
    • 8544240894 scopus 로고    scopus 로고
    • DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication
    • Ishida, T., Akimitsu, N., Kashioka, T., Hatano, M., Kubota, T., Ogata, Y., et al. (2004) DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication. J Biol Chem 279: 45546-45555.
    • (2004) J Biol Chem , vol.279 , pp. 45546-45555
    • Ishida, T.1    Akimitsu, N.2    Kashioka, T.3    Hatano, M.4    Kubota, T.5    Ogata, Y.6
  • 20
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer, L.M., Leipe, D.D., Koonin, E.V., and Aravind, L. (2004) Evolutionary history and higher order classification of AAA+ ATPases. J Struct Biol 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
  • 21
    • 0037515607 scopus 로고    scopus 로고
    • Ordered ATP hydrolysis in the γ complex clamp loader AAA+ machine
    • Johnson, A., and O'Donnell, M. (2003) Ordered ATP hydrolysis in the γ complex clamp loader AAA+ machine. J Biol Chem 278: 14406-14413.
    • (2003) J Biol Chem , vol.278 , pp. 14406-14413
    • Johnson, A.1    O'Donnell, M.2
  • 22
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • Johnson, A., and O'Donnell, M. (2005) Cellular DNA replicases: components and dynamics at the replication fork. Annu Rev Biochem 74: 283-315.
    • (2005) Annu Rev Biochem , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 23
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., Inagawa, T., Wilkinson, A.J., Tatsuta, T., and Ogura, T. (1999) Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J Biol Chem 274: 26225-26232.
    • (1999) J Biol Chem , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 33749239205 scopus 로고    scopus 로고
    • An isolated Hda-clamp complex is functional in the regulatory inactivation of DnaA and DNA replication
    • doi:10.1016/j.jsb.2006.02.007
    • Kawakami, H., Su'etsugu, M., and Katayama, T. (2006) An isolated Hda-clamp complex is functional in the regulatory inactivation of DnaA and DNA replication. J Struct Biol doi:10.1016/j.jsb.2006.02.007.
    • (2006) J Struct Biol
    • Kawakami, H.1    Su'etsugu, M.2    Katayama, T.3
  • 28
    • 0029026635 scopus 로고
    • DNA polymerase III holoenzyme: Structure and function of a chromosomal replicating machine
    • Kelman, Z., and O'Donnell, M. (1995) DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine. Annu Rev Biochem 64: 171-200.
    • (1995) Annu Rev Biochem , vol.64 , pp. 171-200
    • Kelman, Z.1    O'Donnell, M.2
  • 29
    • 0030903098 scopus 로고    scopus 로고
    • Functional domains of Escherichia coli single-stranded DNA binding protein as assessed by analyses of the deletion mutants
    • Kinebuchi, T., Shindo, H., Nagai, H., Shimamoto, N., and Shimizu, M. (1997) Functional domains of Escherichia coli single-stranded DNA binding protein as assessed by analyses of the deletion mutants. Biochemistry 36: 6732-6738.
    • (1997) Biochemistry , vol.36 , pp. 6732-6738
    • Kinebuchi, T.1    Shindo, H.2    Nagai, H.3    Shimamoto, N.4    Shimizu, M.5
  • 30
    • 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., and Bell, S.P. (1997) Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex. Cell 88: 493-502.
    • (1997) Cell , vol.88 , pp. 493-502
    • Klemm, R.D.1    Austin, R.J.2    Bell, S.P.3
  • 31
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models
    • Kopp, J., and Schwede, T. (2004) The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res 32: D230-D234.
    • (2004) Nucleic Acids Res , vol.32
    • Kopp, J.1    Schwede, T.2
  • 32
    • 2442504231 scopus 로고    scopus 로고
    • Interaction of the sliding clamp β-subunit and Hda, a DnaA-related protein
    • Kurz, M., Dalrymple, B., Wijffels, G., and Kongsuwan, K. (2004) Interaction of the sliding clamp β-subunit and Hda, a DnaA-related protein. J Bacteriol 186: 3508-3515.
    • (2004) J Bacteriol , vol.186 , pp. 3508-3515
    • Kurz, M.1    Dalrymple, B.2    Wijffels, G.3    Kongsuwan, K.4
  • 33
    • 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 USA 101: 2811-2816.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2811-2816
    • McGarry, K.C.1    Ryan, V.T.2    Grimwade, J.E.3    Leonard, A.C.4
  • 34
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: Studies of subunit arrangement and functional consequences
    • McHenry, C.S. (2003) Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences. Mol Microbiol 49: 1157-1165
    • (2003) Mol Microbiol , vol.49 , pp. 1157-1165
    • McHenry, C.S.1
  • 35
    • 2442646313 scopus 로고    scopus 로고
    • Requirement for ATP by the DNAdamage checkpoint clamp loader
    • Majka, J., Chung, B.Y., and Burgers, P.M.J. (2004) Requirement for ATP by the DNAdamage checkpoint clamp loader. J Biol Chem 279: 20921-20926.
    • (2004) J Biol Chem , vol.279 , pp. 20921-20926
    • Majka, J.1    Chung, B.Y.2    Burgers, P.M.J.3
  • 36
    • 0025100292 scopus 로고
    • The ABC-primosome. A novel priming system employing dnaA, dnaB, dnaC, and primase on a hairpin containing a dnaA box sequence
    • Masai, H., Nomura, N., and Arai, K. (1990) The ABC-primosome. A novel priming system employing dnaA, dnaB, dnaC, and primase on a hairpin containing a dnaA box sequence. J Biol Chem 265: 15134-15144.
    • (1990) J Biol Chem , vol.265 , pp. 15134-15144
    • Masai, H.1    Nomura, N.2    Arai, K.3
  • 37
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • Messer, W. (2002) The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol Rev 26: 355-374.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 355-374
    • Messer, W.1
  • 38
    • 0026504334 scopus 로고
    • Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit a suppress letD (ccdB) product growth inhibition
    • Miki, T., Park, J.A., Nagao, K., Murayama, N., and Horiuchi, T. (1992) Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit A suppress letD (ccdB) product growth inhibition. J Mol Biol 225: 39-52.
    • (1992) J Mol Biol , vol.225 , pp. 39-52
    • Miki, T.1    Park, J.A.2    Nagao, K.3    Murayama, N.4    Horiuchi, T.5
  • 39
    • 0141707074 scopus 로고    scopus 로고
    • Titration of the Escherichia coli DnaA protein to excess datA sites causes destabilization of replication forks, delayed replication initiation and delayed cell division
    • Morigen, Løbner-Olesen, A., and Skarstad, K. (2003) Titration of the Escherichia coli DnaA protein to excess datA sites causes destabilization of replication forks, delayed replication initiation and delayed cell division. Mol Microbiol 50: 349-362.
    • (2003) Mol Microbiol , vol.50 , pp. 349-362
    • Morigen1    Løbner-Olesen, A.2    Skarstad, K.3
  • 40
    • 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: 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
  • 41
    • 0037177830 scopus 로고    scopus 로고
    • A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication: Evidence 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: evidence 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
  • 42
    • 0036433286 scopus 로고    scopus 로고
    • Determination of the secondary structure in solution of the Escherichia coli DnaA DNA-binding domain
    • Obita, T., Iwura, T., Su'etsugu, M., Yoshida, Y., Tanaka, Y., Katayama, T., et al. (2002) Determination of the secondary structure in solution of the Escherichia coli DnaA DNA-binding domain. Biochem Biophys Res Commun 299: 42-48.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 42-48
    • Obita, T.1    Iwura, T.2    Su'etsugu, M.3    Yoshida, Y.4    Tanaka, Y.5    Katayama, T.6
  • 43
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure - Diverse function
    • + superfamily ATPases: common structure - diverse function. Genes Cells 6: 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 44
    • 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
  • 45
    • 0034975987 scopus 로고    scopus 로고
    • Mutational analysis of conserved sequence motifs in the budding yeast Cdc6 protein
    • Schepers, A., and Diffley, J.F.X. (2001) Mutational analysis of conserved sequence motifs in the budding yeast Cdc6 protein. J Mol Biol 308: 597-608.
    • (2001) J Mol Biol , vol.308 , pp. 597-608
    • Schepers, A.1    Diffley, J.F.X.2
  • 46
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz, H., Weigel, C., and Messer, W. (2000) The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol Microbiol 37: 1270-1279.
    • (2000) Mol Microbiol , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 47
    • 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
  • 48
    • 1942503398 scopus 로고    scopus 로고
    • Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader
    • Seybert, A., and Wigley, D.B. (2004) Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader. EMBO J 23: 1360-1371.
    • (2004) EMBO J , vol.23 , pp. 1360-1371
    • Seybert, A.1    Wigley, D.B.2
  • 49
    • 0942290452 scopus 로고    scopus 로고
    • Hyperinitiation of DNA replication in Escherichia coli leads to replication fork collapse and inviability
    • Simmons, L.A., Breier, A.M., Cozzarelli, N.R., and Kaguni, J.M. (2004) Hyperinitiation of DNA replication in Escherichia coli leads to replication fork collapse and inviability. Mol Microbiol 51: 349-358.
    • (2004) Mol Microbiol , vol.51 , pp. 349-358
    • Simmons, L.A.1    Breier, A.M.2    Cozzarelli, N.R.3    Kaguni, J.M.4
  • 50
    • 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
  • 51
    • 0033229814 scopus 로고    scopus 로고
    • ATP- and ADP-DnaA protein, a molecular switch in gene regulation
    • Speck, C., Weigel, C., and Messer, W. (1999) ATP- and ADP-DnaA protein, a molecular switch in gene regulation. EMBO J 18: 6169-6176.
    • (1999) EMBO J , vol.18 , pp. 6169-6176
    • Speck, C.1    Weigel, C.2    Messer, W.3
  • 52
    • 29544446184 scopus 로고    scopus 로고
    • ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA
    • Speck, C., Chen, Z., Li, H., and Stillman, B. (2005) ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA. Nat Struct Mol Biol 12: 965-971.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 965-971
    • Speck, C.1    Chen, Z.2    Li, H.3    Stillman, B.4
  • 53
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective highlevel expression of cloned genes
    • Studier, F.W., and Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective highlevel expression of cloned genes. J Mol Biol 189: 113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 54
    • 0035038810 scopus 로고    scopus 로고
    • DNA replication-coupled inactivation of DnaA protein in vitro: A role for DnaA arginine-334 of the AAA+ Box VIII motif in ATP hydrolysis
    • Su'etsugu, M., Kawakami, H., Kurokawa, K., Kubota, T., Takata, M., and Katayama, T. (2001) DNA replication-coupled inactivation of DnaA protein in vitro: a role for DnaA arginine-334 of the AAA+ Box VIII motif in ATP hydrolysis. Mol Microbiol 40: 376-386.
    • (2001) Mol Microbiol , vol.40 , pp. 376-386
    • Su'etsugu, M.1    Kawakami, H.2    Kurokawa, K.3    Kubota, T.4    Takata, M.5    Katayama, T.6
  • 55
    • 3042815929 scopus 로고    scopus 로고
    • Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: Interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex
    • Su'etsugu, M., Takata, M., Kubota, T., Matsuda, Y., and Katayama, T. (2004) Molecular mechanism of DNA replication-coupled inactivation of the initiator protein in Escherichia coli: interaction of DnaA with the sliding clamp-loaded DNA and the sliding clamp-Hda complex. Genes Cells 9: 509-522.
    • (2004) Genes Cells , vol.9 , pp. 509-522
    • Su'etsugu, M.1    Takata, M.2    Kubota, T.3    Matsuda, Y.4    Katayama, T.5
  • 56
    • 14844288292 scopus 로고    scopus 로고
    • Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex
    • Su'etsugu, M., Shimuta, T., Ishida, T., Kawakami, H., and Katayama, T. (2005) Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex. J Biol Chem 280: 6528-6536.
    • (2005) J Biol Chem , vol.280 , pp. 6528-6536
    • Su'etsugu, M.1    Shimuta, T.2    Ishida, T.3    Kawakami, H.4    Katayama, T.5
  • 57
    • 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
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 0032844522 scopus 로고    scopus 로고
    • The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA
    • Weigel, C., Schmidt, A., Seitz, H., Tüngler, D., Welzeck, M., and Messer, W. (1999) The N-terminus promotes oligomerization of the Escherichia coli initiator protein DnaA. Mol Microbiol 34: 53-66.
    • (1999) Mol Microbiol , vol.34 , pp. 53-66
    • Weigel, C.1    Schmidt, A.2    Seitz, H.3    Tüngler, D.4    Welzeck, M.5    Messer, W.6


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