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Volumn 51, Issue 2, 2007, Pages 267-275

Expression, purification and characterization of the membrane-associated HrcA repressor protein of Helicobacter pylori

Author keywords

Heat shock; Helicobacter pylori; HrcA expression; HrcA purification

Indexed keywords

REPRESSOR PROTEIN;

EID: 33751529918     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.08.002     Document Type: Article
Times cited : (17)

References (35)
  • 4
    • 0026716505 scopus 로고
    • Urease-associated heat shock protein of Helicobacter pylori
    • Evans D.J., Evans D.G., Engstrand L., and Graham D. Urease-associated heat shock protein of Helicobacter pylori. Infect. Immun. 60 (1992) 2125-2127
    • (1992) Infect. Immun. , vol.60 , pp. 2125-2127
    • Evans, D.J.1    Evans, D.G.2    Engstrand, L.3    Graham, D.4
  • 5
    • 0029848538 scopus 로고    scopus 로고
    • Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA)
    • Kansau I., Guillain F., Thiberge J.M., and Labigne A. Nickel binding and immunological properties of the C-terminal domain of the Helicobacter pylori GroES homologue (HspA). Mol. Microbiol. 22 (1996) 1013-1023
    • (1996) Mol. Microbiol. , vol.22 , pp. 1013-1023
    • Kansau, I.1    Guillain, F.2    Thiberge, J.M.3    Labigne, A.4
  • 7
    • 0029929131 scopus 로고    scopus 로고
    • Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization
    • Huesca M., Borgia S., Hoffman P., and Lingwood C.A. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect. Immun. 64 (1996) 2643-2648
    • (1996) Infect. Immun. , vol.64 , pp. 2643-2648
    • Huesca, M.1    Borgia, S.2    Hoffman, P.3    Lingwood, C.A.4
  • 8
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau B. Regulation of the Escherichia coli heat-shock response. Mol. Microbiol. 9 (1993) 671-680
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 9
    • 33751543918 scopus 로고    scopus 로고
    • C.A. Gross, 1996. Function and regulation of the heat shock proteins in Escherichia coli and Salmonella typhimurium F.C. Niedhardt, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, H.E. Umbarger, (Eds), Cellular and Molecular Biology, American Society for Microbiology, Washington DC, 1996, pp 1382-1399.
  • 10
    • 0032944541 scopus 로고    scopus 로고
    • Negative regulation of bacterial heat shock genes
    • Narberhaus F. Negative regulation of bacterial heat shock genes. Mol. Microbiol. 31 (1999) 1-8
    • (1999) Mol. Microbiol. , vol.31 , pp. 1-8
    • Narberhaus, F.1
  • 11
    • 0030028240 scopus 로고    scopus 로고
    • hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes
    • Schulz A., and Schumann W. hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes. J. Bacteriol. 178 (1996) 1088-1093
    • (1996) J. Bacteriol. , vol.178 , pp. 1088-1093
    • Schulz, A.1    Schumann, W.2
  • 12
    • 0034530509 scopus 로고    scopus 로고
    • The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressor
    • Bucca G., Brassington A.M., Schonfeld H.J., and Smith C.P. The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressor. Mol. Microbiol. 38 (2000) 1093-1103
    • (2000) Mol. Microbiol. , vol.38 , pp. 1093-1103
    • Bucca, G.1    Brassington, A.M.2    Schonfeld, H.J.3    Smith, C.P.4
  • 13
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Helicobacter pylori
    • Tomb J.F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., et al. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388 (1997) 539-547
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.F.1    White, O.2    Kerlavage, A.R.3    Clayton, R.A.4    Sutton, G.G.5
  • 15
    • 0032730207 scopus 로고    scopus 로고
    • The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori
    • Spohn G., and Scarlato V. The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori. Mol. Microbiol. 34 (1999) 663-674
    • (1999) Mol. Microbiol. , vol.34 , pp. 663-674
    • Spohn, G.1    Scarlato, V.2
  • 16
    • 2342495802 scopus 로고    scopus 로고
    • Dual control of Helicobacter pylori heat shock gene transcription by HspR and HrcA
    • Spohn G., Danielli A., Roncarati D., Delany I., Rappuoli R., and Scarlato V. Dual control of Helicobacter pylori heat shock gene transcription by HspR and HrcA. J. Bacteriol. 186 (2004) 2956-2965
    • (2004) J. Bacteriol. , vol.186 , pp. 2956-2965
    • Spohn, G.1    Danielli, A.2    Roncarati, D.3    Delany, I.4    Rappuoli, R.5    Scarlato, V.6
  • 17
    • 0033988198 scopus 로고    scopus 로고
    • Role of HrcA and CIRCE in the heat shock regulatory network of Bradyrhizobium japonicum
    • Minder A.C., Fischer H.M., Hennecke H., and Narberhaus F. Role of HrcA and CIRCE in the heat shock regulatory network of Bradyrhizobium japonicum. J. Bacteriol. 182 (2000) 14-22
    • (2000) J. Bacteriol. , vol.182 , pp. 14-22
    • Minder, A.C.1    Fischer, H.M.2    Hennecke, H.3    Narberhaus, F.4
  • 18
    • 0036889034 scopus 로고    scopus 로고
    • Functional analysis of the heat shock regulator HrcA of Chlamydia trachomatis
    • Wilson A.C., and Tan M. Functional analysis of the heat shock regulator HrcA of Chlamydia trachomatis. J. Bacteriol. 184 (2002) 6566-6571
    • (2002) J. Bacteriol. , vol.184 , pp. 6566-6571
    • Wilson, A.C.1    Tan, M.2
  • 19
    • 4944247158 scopus 로고    scopus 로고
    • Functional and structural analysis of HrcA repressor protein from Caulobacter crescentus
    • Susin M.F., Perez H.R., Baldini R.L., and Gomes S.L. Functional and structural analysis of HrcA repressor protein from Caulobacter crescentus. J. Bacteriol. 186 (2004) 6759-6767
    • (2004) J. Bacteriol. , vol.186 , pp. 6759-6767
    • Susin, M.F.1    Perez, H.R.2    Baldini, R.L.3    Gomes, S.L.4
  • 20
    • 0037031815 scopus 로고    scopus 로고
    • Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE function
    • Rieschl S., Wiegert T., and Schumann W. Isolation and analysis of mutant alleles of the Bacillus subtilis HrcA repressor with reduced dependency on GroE function. J. Biol. Chem. 277 (2002) 32659-32667
    • (2002) J. Biol. Chem. , vol.277 , pp. 32659-32667
    • Rieschl, S.1    Wiegert, T.2    Schumann, W.3
  • 21
    • 0035192005 scopus 로고    scopus 로고
    • Renaturation of Bacillus thermoglucosidasius HrcA repressor by DNA and thermostability of the HrcA-DNA complexes in vitro
    • Watanabe K., Yamamoto T., and Suzuki Y. Renaturation of Bacillus thermoglucosidasius HrcA repressor by DNA and thermostability of the HrcA-DNA complexes in vitro. J. Bacteriol. 183 (2001) 155-161
    • (2001) J. Bacteriol. , vol.183 , pp. 155-161
    • Watanabe, K.1    Yamamoto, T.2    Suzuki, Y.3
  • 23
    • 0031854047 scopus 로고    scopus 로고
    • Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae
    • Crawford J.A., Kaper J.B., and DiRita V.J. Analysis of ToxR-dependent transcription activation of ompU, the gene encoding a major envelope protein in Vibrio cholerae. Mol. Microbiol. 29 (1998) 235-246
    • (1998) Mol. Microbiol. , vol.29 , pp. 235-246
    • Crawford, J.A.1    Kaper, J.B.2    DiRita, V.J.3
  • 24
    • 27744481253 scopus 로고    scopus 로고
    • In vitro analysis of protein-operator interactions of the NikR and Fur metal-responsive regulators of coregulated genes in Helicobacter pylori
    • Delany I., Ieva R., Soragni A., Hilleringmann M., Rappuoli R., and Scarlato V. In vitro analysis of protein-operator interactions of the NikR and Fur metal-responsive regulators of coregulated genes in Helicobacter pylori. J. Bacteriol. 187 (2005) 7703-7715
    • (2005) J. Bacteriol. , vol.187 , pp. 7703-7715
    • Delany, I.1    Ieva, R.2    Soragni, A.3    Hilleringmann, M.4    Rappuoli, R.5    Scarlato, V.6
  • 25
    • 0033815224 scopus 로고    scopus 로고
    • The Vibrio cholerae ToxR/TcpP/ToxT virulence cascade: distinct roles for two membrane-localized transcriptional activators on a single promoter
    • Krukonis E.S., Yu R.R., and DiRita V.J. The Vibrio cholerae ToxR/TcpP/ToxT virulence cascade: distinct roles for two membrane-localized transcriptional activators on a single promoter. Mol. Microbiol. 38 (2000) 67-84
    • (2000) Mol. Microbiol. , vol.38 , pp. 67-84
    • Krukonis, E.S.1    Yu, R.R.2    DiRita, V.J.3
  • 26
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller V.L., Taylor R.K., and Mekalanos J.J. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell 48 (1987) 271-279
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 27
    • 0033988967 scopus 로고    scopus 로고
    • A region of the transmembrane regulatory protein ToxR that tethers the transcriptional activation domain to the cytoplasmic membrane displays wide divergence among Vibrio species
    • Osorio C.R., and Klose K.E. A region of the transmembrane regulatory protein ToxR that tethers the transcriptional activation domain to the cytoplasmic membrane displays wide divergence among Vibrio species. J. Bacteriol. 182 (1999) 526-529
    • (1999) J. Bacteriol. , vol.182 , pp. 526-529
    • Osorio, C.R.1    Klose, K.E.2
  • 29
    • 0030849142 scopus 로고    scopus 로고
    • The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
    • Mogk A., Homuth G., Scholz C., Kim L., Schmid F.X., and Schumann W. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J. 16 (1997) 4579-4590
    • (1997) EMBO J. , vol.16 , pp. 4579-4590
    • Mogk, A.1    Homuth, G.2    Scholz, C.3    Kim, L.4    Schmid, F.X.5    Schumann, W.6
  • 30
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166 (1983) 557-580
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 31
    • 0023840230 scopus 로고
    • ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg J., and Dunn J.J. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J. Bacteriol. 170 (1988) 1245-1253
    • (1988) J. Bacteriol. , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 32
    • 0028860071 scopus 로고
    • Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin
    • Xiang Z., Censini S., Bayeli P.F., Telford J.L., Figura N., Rappuoli R., and Covacci A. Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin. Infect. Immun. 63 (1995) 94-98
    • (1995) Infect. Immun. , vol.63 , pp. 94-98
    • Xiang, Z.1    Censini, S.2    Bayeli, P.F.3    Telford, J.L.4    Figura, N.5    Rappuoli, R.6    Covacci, A.7
  • 33
    • 1842297740 scopus 로고
    • Shuttle mutagenesis: a method of transposon mutagenesis for Saccharomyces cerevisiae
    • Seifert H.S., Chen E.Y., So M., and Heffron F. Shuttle mutagenesis: a method of transposon mutagenesis for Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 83 (1986) 735-739
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 735-739
    • Seifert, H.S.1    Chen, E.Y.2    So, M.3    Heffron, F.4
  • 34
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S., and Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82 (1985) 1074-1078
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 35
    • 0036718563 scopus 로고    scopus 로고
    • Growth phase dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori
    • Delany I., Spohn G., Rappuoli R., and Scarlato V. Growth phase dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori. J. Bacteriol. 184 (2002) 4800-4810
    • (2002) J. Bacteriol. , vol.184 , pp. 4800-4810
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.