메뉴 건너뛰기




Volumn 37, Issue 13, 2009, Pages 4441-4452

A biochemically active MCM-like helicase in Bacillus cereus

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; HELICASE; MINI CHROMOSOME MAINTENANCE PROTEIN; UNCLASSIFIED DRUG;

EID: 67949102098     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp376     Document Type: Article
Times cited : (8)

References (49)
  • 1
    • 1542405310 scopus 로고    scopus 로고
    • Eukaryotic MCM proteins: Beyond replication initiation
    • Forsburg,S.L. (2004) Eukaryotic MCM proteins: Beyond replication initiation. Microbiol. Mol. Biol. Rev., 68, 109-131.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 109-131
    • Forsburg, S.L.1
  • 2
    • 64149093563 scopus 로고    scopus 로고
    • Unwinding the structure and function of the archaeal MCM helicase
    • Sakakibara,N., Kelman,L.M. and Kelman,Z. (2009) Unwinding the structure and function of the archaeal MCM helicase. Mol. Microbiol., 72 286-296.
    • (2009) Mol. Microbiol , vol.72 , pp. 286-296
    • Sakakibara, N.1    Kelman, L.M.2    Kelman, Z.3
  • 3
    • 29244451896 scopus 로고    scopus 로고
    • The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding
    • Ying,C.Y. and Gautier,J. (2005) The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding. EMBO J., 24, 4334-4344.
    • (2005) EMBO J , vol.24 , pp. 4334-4344
    • Ying, C.Y.1    Gautier, J.2
  • 4
    • 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. and Botchan,M.R. (2006) Isolation of the Cdc45/ Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc. Natl Acad. Sci. USA, 103, 10236-10241.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10236-10241
    • Moyer, S.E.1    Lewis, P.W.2    Botchan, M.R.3
  • 5
    • 32444450705 scopus 로고    scopus 로고
    • Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication
    • Pacek,M., Tutter,A.V., Kubota,Y., Takisawa,H. and Walter,J.C. (2006) Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication. Mol. Cell, 21, 581-587.
    • (2006) Mol. Cell , vol.21 , pp. 581-587
    • Pacek, M.1    Tutter, A.V.2    Kubota, Y.3    Takisawa, H.4    Walter, J.C.5
  • 6
    • 0030859463 scopus 로고    scopus 로고
    • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex
    • Ishimi, Y. (1997) A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. J. Biol. Chem., 272, 24508-24513.
    • (1997) J. Biol. Chem , vol.272 , pp. 24508-24513
    • Ishimi, Y.1
  • 7
    • 0038475879 scopus 로고    scopus 로고
    • Reconstitution of the mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture
    • Davey,M.J., Indiani,C. and O'Donnell,M. (2003) Reconstitution of the mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture. J. Biol. Chem., 278, 4491-4499.
    • (2003) J. Biol. Chem , vol.278 , pp. 4491-4499
    • Davey, M.J.1    Indiani, C.2    O'Donnell, M.3
  • 8
    • 57649171240 scopus 로고    scopus 로고
    • Mcm subunits can assemble into two different active unwinding complexes
    • Kanter,D.M., Bruck,I. and Kaplan,D.L. (2008) Mcm subunits can assemble into two different active unwinding complexes. J. Biol. Chem., 283, 31172-31182.
    • (2008) J. Biol. Chem , vol.283 , pp. 31172-31182
    • Kanter, D.M.1    Bruck, I.2    Kaplan, D.L.3
  • 9
    • 47349114465 scopus 로고    scopus 로고
    • The Mcm2-7 complex has in vitro helicase activity
    • Bochman,M.L. and Schwacha,A. (2008) The Mcm2-7 complex has in vitro helicase activity. Mol. Cell, 31, 287-293.
    • (2008) Mol. Cell , vol.31 , pp. 287-293
    • Bochman, M.L.1    Schwacha, A.2
  • 11
    • 45549086385 scopus 로고    scopus 로고
    • Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain
    • PMCID: 2425480
    • Lium, W., Pucci,B., Rossi,M., Pisani,F.M. and Ladenstein,R. (2008) Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain. Nucleic Acids Res., 36, 3235-3243. [PMCID: 2425480].
    • (2008) Nucleic Acids Res , vol.36 , pp. 3235-3243
    • Lium, W.1    Pucci, B.2    Rossi, M.3    Pisani, F.M.4    Ladenstein, R.5
  • 12
    • 0035965990 scopus 로고    scopus 로고
    • The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity
    • Poplawski,A., Grabowski,B., Long,S.E. and Kelman,Z. (2001) The zinc finger domain of the archaeal minichromosome maintenance protein is required for helicase activity. J. Biol. Chem., 276, 49371-49377.
    • (2001) J. Biol. Chem , vol.276 , pp. 49371-49377
    • Poplawski, A.1    Grabowski, B.2    Long, S.E.3    Kelman, Z.4
  • 13
    • 57649119780 scopus 로고    scopus 로고
    • Biochemical characterization of the minichromosome maintenance (MCM) protein of the crenarchaeote Aeropyrum pernix and its interactions with the origin recognition complex (ORC) proteins
    • Atanassova,N. and Grainge,I. (2008) Biochemical characterization of the minichromosome maintenance (MCM) protein of the crenarchaeote Aeropyrum pernix and its interactions with the origin recognition complex (ORC) proteins. Biochemistry., 47, 13362-13370.
    • (2008) Biochemistry , vol.47 , pp. 13362-13370
    • Atanassova, N.1    Grainge, I.2
  • 15
    • 33845648483 scopus 로고    scopus 로고
    • Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity
    • Costa,A., Pape, T., van Heel,M., Brick,P., Patwardhan,A. and Onesti,S. (2006) Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity. Nucleic Acids Res., 34, 5829-5838.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5829-5838
    • Costa, A.1    Pape, T.2    van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 16
    • 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. and Bell,S.D. (2005) Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism. Nat. Struct. Mol. Biol.
    • (2005) Nat. Struct. Mol. Biol
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 17
    • 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
  • 18
    • 28244461615 scopus 로고    scopus 로고
    • Identification of full genes and proteins of MCM9, a novel, vertebrate-specific member of the MCM2-8 protein family
    • Lutzmann,M., Maiorano,D. and Mechali,M. (2005) Identification of full genes and proteins of MCM9, a novel, vertebrate-specific member of the MCM2-8 protein family. Gene., 362, 51-56.
    • (2005) Gene , vol.362 , pp. 51-56
    • Lutzmann, M.1    Maiorano, D.2    Mechali, M.3
  • 19
    • 13544252547 scopus 로고    scopus 로고
    • MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation
    • Maiorano,D., Cuvier,O., Danis,E. and Mechali,M. (2005) MCM8 is an MCM2-7-related protein that functions as a DNA helicase during replication elongation and not initiation. Cell, 120, 315-328.
    • (2005) Cell , vol.120 , pp. 315-328
    • Maiorano, D.1    Cuvier, O.2    Danis, E.3    Mechali, M.4
  • 21
    • 0348133607 scopus 로고    scopus 로고
    • Hexameric ring structure of the full-length archaeal MCM protein complex
    • Pape,T., Meka,H., Chen,S., Vicentini,G., Van Heel,M. and Onesti,S. (2003) Hexameric ring structure of the full-length archaeal MCM protein complex. EMBO Rep., 4, 1079-1083.
    • (2003) EMBO Rep , vol.4 , pp. 1079-1083
    • Pape, T.1    Meka, H.2    Chen, S.3    Vicentini, G.4    Van Heel, M.5    Onesti, S.6
  • 22
    • 33749266161 scopus 로고    scopus 로고
    • Structural studies of the archaeal MCM complex in different functional states
    • Costa,A., Pape,T., van Heel,M., Brick,P., Patwardhan,A. and Onesti,S. (2006) Structural studies of the archaeal MCM complex in different functional states. J. Struct. Biol., 156, 210-219.
    • (2006) J. Struct. Biol , vol.156 , pp. 210-219
    • Costa, A.1    Pape, T.2    van Heel, M.3    Brick, P.4    Patwardhan, A.5    Onesti, S.6
  • 24
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey,S., Eliason, W.K. and Steitz, T.A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science. 318, 459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 25
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark,E.J. and Joshua-Tor,L. (2006) Mechanism of DNA translocation in a replicative hexameric helicase. Nature., 442, 270-275.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 26
    • 59649110896 scopus 로고    scopus 로고
    • Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog
    • Bae,B., Chen, Y., Costa,A., Onesti,S., Brunzelle,J., Lin, Y., Cann,I. and Nair,S. (2009) Insights into the architecture of the replicative helicase from the structure of an archaeal MCM homolog. Structure, 17, 211-22.
    • (2009) Structure , vol.17 , pp. 211-222
    • Bae, B.1    Chen, Y.2    Costa, A.3    Onesti, S.4    Brunzelle, J.5    Lin, Y.6    Cann, I.7    Nair, S.8
  • 28
    • 12944319325 scopus 로고    scopus 로고
    • Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome
    • McGeoch,A.T. and Bell,S.D. (2005) Eukaryotic/archaeal primase and MCM proteins encoded in a bacteriophage genome. Cell, 120, 167-168.
    • (2005) Cell , vol.120 , pp. 167-168
    • McGeoch, A.T.1    Bell, S.D.2
  • 29
    • 22444435033 scopus 로고    scopus 로고
    • Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: Structural insights and new members
    • Iyer,L.M., Koonin,E.V., Leipe,D.D. and Aravind,L. (2005) Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: Structural insights and new members. Nucleic Acids Res., 33, 3875-3896.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3875-3896
    • Iyer, L.M.1    Koonin, E.V.2    Leipe, D.D.3    Aravind, L.4
  • 30
    • 33845466226 scopus 로고    scopus 로고
    • Shin,J.H. and Kelman,Z. (2006) DNA unwinding assay using streptavidin-bound oligonucleotides. BMC Mol. Biol., 7, 43.
    • Shin,J.H. and Kelman,Z. (2006) DNA unwinding assay using streptavidin-bound oligonucleotides. BMC Mol. Biol., 7, 43.
  • 31
    • 0141737560 scopus 로고    scopus 로고
    • NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities
    • Kiianitsa,K., Solinger,J.A. and Heyer, W.D. (2003) NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities. Anal. Biochem., 321, 266-271.
    • (2003) Anal. Biochem , vol.321 , pp. 266-271
    • Kiianitsa, K.1    Solinger, J.A.2    Heyer, W.D.3
  • 32
    • 0018101448 scopus 로고
    • Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains
    • Rowen,L. and Kornberg,A. (1978) Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J. Biol. Chem., 253 758-764.
    • (1978) J. Biol. Chem , vol.253 , pp. 758-764
    • Rowen, L.1    Kornberg, A.2
  • 33
    • 38349057357 scopus 로고    scopus 로고
    • Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding
    • Pakotiprapha,D., Inuzuka,Y., Bowman,B.R., Moolenaar,G.F., Goosen,N., Jeruzalmi,D. and Verdine,G.L. (2008) Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Mol. Cell, 29 122-133.
    • (2008) Mol. Cell , vol.29 , pp. 122-133
    • Pakotiprapha, D.1    Inuzuka, Y.2    Bowman, B.R.3    Moolenaar, G.F.4    Goosen, N.5    Jeruzalmi, D.6    Verdine, G.L.7
  • 34
    • 0037616144 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex
    • Galletto,R., Jezewska,M.J. and Bujalowski,W. (2003) Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex. J. Mol. Biol., 329, 441-465.
    • (2003) J. Mol. Biol , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 35
    • 0031019643 scopus 로고    scopus 로고
    • Learn,B.A., Um,S.J., Huang,L. and McMacken,R. (1997) Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA. Proc. Natl Acad. Sci. USA 94, 1154-1159.
    • Learn,B.A., Um,S.J., Huang,L. and McMacken,R. (1997) Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA. Proc. Natl Acad. Sci. USA 94, 1154-1159.
  • 36
    • 0019490027 scopus 로고
    • Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication
    • Arai,K. and Kornberg,A. (1981) Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication. J. Biol. Chem., 256, 5260-5266.
    • (1981) J. Biol. Chem , vol.256 , pp. 5260-5266
    • Arai, K.1    Kornberg, A.2
  • 37
    • 0019400815 scopus 로고
    • Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA
    • Arai,K. and Kornberg,A. (1981) Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA. J. Biol. Chem., 256, 5253-5259.
    • (1981) J. Biol. Chem , vol.256 , pp. 5253-5259
    • Arai, K.1    Kornberg, A.2
  • 38
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • Wyatt,P. (1993) Light scattering and the absolute characterization of macromolecules. Analytica Chimica Acta, 272, 1-40.
    • (1993) Analytica Chimica Acta , vol.272 , pp. 1-40
    • Wyatt, P.1
  • 41
    • 1642524959 scopus 로고    scopus 로고
    • Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases
    • Steitz,T.A. and Yin,Y.W. (2004) Accuracy, lesion bypass, strand displacement and translocation by DNA polymerases. Philos Trans R Soc Lond, B, Biol. Sci., 359, 17-23.
    • (2004) Philos Trans R Soc Lond, B, Biol. Sci , vol.359 , pp. 17-23
    • Steitz, T.A.1    Yin, Y.W.2
  • 42
    • 0344012482 scopus 로고    scopus 로고
    • Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus
    • PMCID: 169903
    • Grainge,I., Scaife,S. and Wigley,D.B. (2003) Biochemical analysis of components of the pre-replication complex of Archaeoglobus fulgidus. Nucleic Acids Res., 31, 4888-4898. PMCID: 169903.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4888-4898
    • Grainge, I.1    Scaife, S.2    Wigley, D.B.3
  • 43
    • 33847376397 scopus 로고    scopus 로고
    • Archaeal MCM has separable processivity, substrate choice and helicase domains
    • Barry,E.R., McGeoch,A.T., Kelman,Z. and Bell,S.D. (2007) Archaeal MCM has separable processivity, substrate choice and helicase domains. Nucleic Acids Res., 35, 988-998.
    • (2007) Nucleic Acids Res , vol.35 , pp. 988-998
    • Barry, E.R.1    McGeoch, A.T.2    Kelman, Z.3    Bell, S.D.4
  • 44
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton,M.R., Sawaya,M.R., Ellenberger,T. and Wigley,D.B. (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell, 101, 589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 45
    • 0026770783 scopus 로고
    • The simian virus 40 T antigen double hexamer assembles around the DNA at the replication origin
    • Dean,F.B., Borowiec,J.A., Eki,T. and Hurwitz,J. (1992) The simian virus 40 T antigen double hexamer assembles around the DNA at the replication origin. J. Biol. Chem., 267, 14129-14137.
    • (1992) J. Biol. Chem , vol.267 , pp. 14129-14137
    • Dean, F.B.1    Borowiec, J.A.2    Eki, T.3    Hurwitz, J.4
  • 46
    • 0042200759 scopus 로고    scopus 로고
    • Replicative helicase loaders: Ring breakers and ring makers
    • Davey,M.J. and O'Donnell,M. (2003) Replicative helicase loaders: Ring breakers and ring makers. Curr. Biol., 13, R594-R596.
    • (2003) Curr. Biol , vol.13
    • Davey, M.J.1    O'Donnell, M.2
  • 47
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • PMCID: 390337
    • Edgar,R.C. (2004) MUSCLE: Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res., 32, 1792-1797. PMCID: 390337.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 48
    • 0034843597 scopus 로고    scopus 로고
    • AL2CO: Calculation of positional conservation in a protein sequence alignment
    • Pei,J. and Grishin,N.V. (2001) AL2CO: Calculation of positional conservation in a protein sequence alignment. Bioinformatics., 17, 700-712.
    • (2001) Bioinformatics , vol.17 , pp. 700-712
    • Pei, J.1    Grishin, N.V.2
  • 49
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff,S. and Henikoff,J.G. (1992) Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA, 89, 10915-10919.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.