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Volumn 77, Issue 5, 2010, Pages 1289-1300

Dimerization and DNA-dependent aggregation of the Escherichia coli nucleoid protein and chaperone CbpA

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN CBPA; UNCLASSIFIED DRUG;

EID: 77956155529     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07292.x     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón, M., Link, A.J., Furlong, D. Kolter, R. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6 : 2646 2654.
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 2
    • 0032731196 scopus 로고    scopus 로고
    • Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity
    • Azam, T.A. Ishihama, A. (1999) Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. J Biol Chem 274 : 33105 33113.
    • (1999) J Biol Chem , vol.274 , pp. 33105-33113
    • Azam, T.A.1    Ishihama, A.2
  • 3
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Azam, T.A., Iwata, A., Nishimura, A., Ueda, S. Ishihama, A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J Bacteriol 181 : 6361 6370.
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Azam, T.A.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 4
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam, T.A., Hiraga, S. Ishihama, A. (2000) Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes Cells 5 : 613 626.
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.A.1    Hiraga, S.2    Ishihama, A.3
  • 5
    • 33845922099 scopus 로고    scopus 로고
    • Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein
    • Bird, J.G., Sharma, S., Roshwalb, S.C., Hoskins, J.R. Wickner, S. (2006) Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein. J Biol Chem 281 : 34349 34356.
    • (2006) J Biol Chem , vol.281 , pp. 34349-34356
    • Bird, J.G.1    Sharma, S.2    Roshwalb, S.C.3    Hoskins, J.R.4    Wickner, S.5
  • 6
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci, P., Cellai, S., Falvo, E., Rivetti, C., Rossi, G.L. Chiancone, E. (2004) DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus. Nucleic Acids Res 32 : 5935 5944.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 7
    • 4043103993 scopus 로고    scopus 로고
    • CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM
    • Chae, C., Sharma, S., Hoskins, J.R. Wickner, S. (2004) CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM. J Biol Chem 279 : 33147 33153.
    • (2004) J Biol Chem , vol.279 , pp. 33147-33153
    • Chae, C.1    Sharma, S.2    Hoskins, J.R.3    Wickner, S.4
  • 8
    • 48149104997 scopus 로고    scopus 로고
    • Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM
    • Chenoweth, M.R. Wickner, S. (2008) Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM. J Bacteriol 190 : 5153 5161.
    • (2008) J Bacteriol , vol.190 , pp. 5153-5161
    • Chenoweth, M.R.1    Wickner, S.2
  • 9
    • 34247632202 scopus 로고    scopus 로고
    • In vivo modulation of a DnaJ homolog, CbpA, by CbpM
    • Chenoweth, M.R., Trun, N. Wickner, S. (2007) In vivo modulation of a DnaJ homolog, CbpA, by CbpM. J Bacteriol 189 : 3635 3638.
    • (2007) J Bacteriol , vol.189 , pp. 3635-3638
    • Chenoweth, M.R.1    Trun, N.2    Wickner, S.3
  • 10
    • 76949089832 scopus 로고    scopus 로고
    • Bacterial nucleoid-associated proteins, nucleoid structure and gene expression
    • Dillon, S.C. 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
  • 11
    • 60649108870 scopus 로고    scopus 로고
    • Nucleoid-associated proteins and bacterial physiology
    • Dorman, C.J. (2009) Nucleoid-associated proteins and bacterial physiology. Adv Appl Microbiol 67 : 47 64.
    • (2009) Adv Appl Microbiol , vol.67 , pp. 47-64
    • Dorman, C.J.1
  • 12
    • 33750000118 scopus 로고    scopus 로고
    • Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome
    • Grainger, D.C., Hurd, D., Goldberg, M.D. Busby, S.J. (2006) Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome. Nucleic Acids Res 34 : 4642 4652.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4642-4652
    • Grainger, D.C.1    Hurd, D.2    Goldberg, M.D.3    Busby, S.J.4
  • 13
    • 44249126516 scopus 로고    scopus 로고
    • Selective repression by Fis and H-NS at the Escherichia coli dps promoter
    • Grainger, D.C., Goldberg, M.D., Lee, D.J. Busby, S.J. (2008) Selective repression by Fis and H-NS at the Escherichia coli dps promoter. Mol Microbiol 68 : 1366 1377.
    • (2008) Mol Microbiol , vol.68 , pp. 1366-1377
    • Grainger, D.C.1    Goldberg, M.D.2    Lee, D.J.3    Busby, S.J.4
  • 14
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R. Hogle, J.M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struct Biol 5 : 294 303.
    • (1998) Nat Struct Biol , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 15
    • 33750529760 scopus 로고    scopus 로고
    • Coupling the distribution of RNA polymerase to global gene regulation and the dynamic structure of the bacterial nucleoid in Escherichia coli
    • Jin, D.J. Cabrera, J.E. (2006) Coupling the distribution of RNA polymerase to global gene regulation and the dynamic structure of the bacterial nucleoid in Escherichia coli. J Struct Biol 156 : 284 291.
    • (2006) J Struct Biol , vol.156 , pp. 284-291
    • Jin, D.J.1    Cabrera, J.E.2
  • 16
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A. Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc Natl Acad Sci USA 95 : 5752 5756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 17
    • 0035151432 scopus 로고    scopus 로고
    • Protein-protein interaction between Bacillus stearothermophilus tyrosyl tRNA synthetase subdomains revealed by a bacterial two-hybrid system
    • Karimova, G., Ullmann, A. Ladant, D. (2001) Protein-protein interaction between Bacillus stearothermophilus tyrosyl tRNA synthetase subdomains revealed by a bacterial two-hybrid system. J Mol Microbiol Biotechnol 3 : 73 82.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 73-82
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 18
    • 3042660143 scopus 로고    scopus 로고
    • Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy
    • Kim, J., Yoshimura, S.H., Hizume, K., Ohniwa, R.L., Ishihama, A. Takeyasu, K. (2004) Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy. Nucleic Acids Res 32 : 1982 1992.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1982-1992
    • Kim, J.1    Yoshimura, S.H.2    Hizume, K.3    Ohniwa, R.L.4    Ishihama, A.5    Takeyasu, K.6
  • 19
    • 76449095971 scopus 로고    scopus 로고
    • Nuclear-encoded DnaJ homolog of Plasmodium falciparum interacts with replication ori of the apicoplast genome
    • Kumar, A., Tanveer, A., Biswas, S., Ram, E.R., Gupta, A., Kumar, B. Habib, S. (2010) Nuclear-encoded DnaJ homolog of Plasmodium falciparum interacts with replication ori of the apicoplast genome. Mol Microbiol 75 : 942 956.
    • (2010) Mol Microbiol , vol.75 , pp. 942-956
    • Kumar, A.1    Tanveer, A.2    Biswas, S.3    Ram, E.R.4    Gupta, A.5    Kumar, B.6    Habib, S.7
  • 20
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press
    • Miller, J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.1
  • 21
    • 33751580332 scopus 로고    scopus 로고
    • Dynamic state of DNA topology is essential for genome condensation in bacteria
    • Ohniwa, R.L., Morikawa, K., Kim, J., Ohta, T., Ishihama, A., Wada, C. Takeyasu, K. (2006) Dynamic state of DNA topology is essential for genome condensation in bacteria. EMBO J 25 : 5591 5602.
    • (2006) EMBO J , vol.25 , pp. 5591-5602
    • Ohniwa, R.L.1    Morikawa, K.2    Kim, J.3    Ohta, T.4    Ishihama, A.5    Wada, C.6    Takeyasu, K.7
  • 22
    • 0025128277 scopus 로고
    • Different physiological roles of two independent pathways for nitrite reduction to ammonia by enteric bacteria
    • Page, L., Griffiths, L. Cole, J.A. (1990) Different physiological roles of two independent pathways for nitrite reduction to ammonia by enteric bacteria. Arch Microbiol 154 : 349 354.
    • (1990) Arch Microbiol , vol.154 , pp. 349-354
    • Page, L.1    Griffiths, L.2    Cole, J.A.3
  • 24
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • Sha, B., Lee, S. Cyr, D. (2000) The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 8 : 799 807.
    • (2000) Structure , vol.8 , pp. 799-807
    • Sha, B.1    Lee, S.2    Cyr, D.3
  • 25
    • 0027979545 scopus 로고
    • An analogue of the DnaJ molecular chaperone in Escherichia coli
    • Ueguchi, C., Kakeda, M., Yamada, H. Mizuno, T. (1994) An analogue of the DnaJ molecular chaperone in Escherichia coli. Proc Natl Acad Sci USA 91 : 1054 1058.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1054-1058
    • Ueguchi, C.1    Kakeda, M.2    Yamada, H.3    Mizuno, T.4
  • 26
    • 0029034167 scopus 로고
    • A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
    • Ueguchi, C., Shiozawa, T., Kakeda, M., Yamada, H. Mizuno, T. (1995) A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J Bacteriol 177 : 3894 3896.
    • (1995) J Bacteriol , vol.177 , pp. 3894-3896
    • Ueguchi, C.1    Shiozawa, T.2    Kakeda, M.3    Yamada, H.4    Mizuno, T.5
  • 27
    • 77956155798 scopus 로고    scopus 로고
    • PhD Thesis, University of Birmingham, UK
    • Westblade, L.F. (2004) PhD Thesis. University of Birmingham, UK.
    • (2004)
    • Westblade, L.F.1
  • 29
    • 0025003429 scopus 로고
    • An Escherichia coli protein that preferentially binds to sharply curved DNA
    • Yamada, H., Muramatsu, S. Mizuno, T. (1990) An Escherichia coli protein that preferentially binds to sharply curved DNA. J Biochem 108 : 420 425.
    • (1990) J Biochem , vol.108 , pp. 420-425
    • Yamada, H.1    Muramatsu, S.2    Mizuno, T.3
  • 30
    • 33750510057 scopus 로고    scopus 로고
    • Shape and compaction of Escherichia coli nucleoids
    • Zimmerman, S.B. (2006) Shape and compaction of Escherichia coli nucleoids. J Struct Biol 156 : 255 261.
    • (2006) J Struct Biol , vol.156 , pp. 255-261
    • Zimmerman, S.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.