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Volumn 302, Issue 6, 2012, Pages 242-252

An insight into the significance of the DnaK heat shock system in Staphylococcus aureus

Author keywords

DnaK; Heat shock protein; Staphylococcus

Indexed keywords

ANTIBIOTIC AGENT; CAROTENOID; HEAT SHOCK PROTEIN; PROTEIN DNAK;

EID: 84867867543     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2012.05.001     Document Type: Article
Times cited : (42)

References (41)
  • 1
    • 0037634030 scopus 로고    scopus 로고
    • Mutation of sarA in Staphylococcus aureus limits biofilm formation
    • Beenken K.E., Blevins J.S., Smeltzer M.S. Mutation of sarA in Staphylococcus aureus limits biofilm formation. Infect. Immun. 2003, 71:4206-4211.
    • (2003) Infect. Immun. , vol.71 , pp. 4206-4211
    • Beenken, K.E.1    Blevins, J.S.2    Smeltzer, M.S.3
  • 3
    • 34447540214 scopus 로고    scopus 로고
    • Acid-shock responses in Staphylococcus aureus investigated by global gene expression analysis
    • Bore E., Langsrud S., Langsrud O., Rode T.M., Holck A. Acid-shock responses in Staphylococcus aureus investigated by global gene expression analysis. Microbiology 2007, 153:2289-2303.
    • (2007) Microbiology , vol.153 , pp. 2289-2303
    • Bore, E.1    Langsrud, S.2    Langsrud, O.3    Rode, T.M.4    Holck, A.5
  • 4
    • 0031725420 scopus 로고    scopus 로고
    • The Staphylococcus aureus alternative sigma factor SigmaB controls the environmental stress response but not starvation survival or pathogenicity in a mouse abscess model
    • Chan P.F., Foster S.J., Ingham E., Clements M.O. The Staphylococcus aureus alternative sigma factor SigmaB controls the environmental stress response but not starvation survival or pathogenicity in a mouse abscess model. J. Bacteriol. 1998, 180:6082-6089.
    • (1998) J. Bacteriol. , vol.180 , pp. 6082-6089
    • Chan, P.F.1    Foster, S.J.2    Ingham, E.3    Clements, M.O.4
  • 5
    • 44649169371 scopus 로고    scopus 로고
    • Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation
    • Chang Y.W., Sun Y.J., Wang C., Hsiao C.D. Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J. Biol. Chem. 2008, 283:15502-15511.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15502-15511
    • Chang, Y.W.1    Sun, Y.J.2    Wang, C.3    Hsiao, C.D.4
  • 6
    • 0037329158 scopus 로고    scopus 로고
    • Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria
    • Chastanet A., Fert J., Msadek T. Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria. Mol. Microbiol. 2003, 47:1061-1073.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1061-1073
    • Chastanet, A.1    Fert, J.2    Msadek, T.3
  • 7
    • 21144455573 scopus 로고    scopus 로고
    • Staphylococcus aureus ClpC is required for stress resistance, aconitase activity, growth recovery, and death
    • Chatterjee I., Becker P., Grundmeier M., other authors Staphylococcus aureus ClpC is required for stress resistance, aconitase activity, growth recovery, and death. J. Bacteriol. 2005, 187:4488-4496.
    • (2005) J. Bacteriol. , vol.187 , pp. 4488-4496
    • Chatterjee, I.1    Becker, P.2    Grundmeier, M.3
  • 8
    • 0033230566 scopus 로고    scopus 로고
    • Stress resistance in Staphylococcus aureus
    • Clements M.O., Foster S.J. Stress resistance in Staphylococcus aureus. Trends Microbiol. 1999, 7:458-462.
    • (1999) Trends Microbiol. , vol.7 , pp. 458-462
    • Clements, M.O.1    Foster, S.J.2
  • 10
    • 78651543474 scopus 로고    scopus 로고
    • Induction kinetics of the Staphylococcus aureus cell wall stress stimulon in response to different cell wall active antibiotics
    • Dengler V., Meier P.S., Heusser R., Berger-Bachi B., McCallum N. Induction kinetics of the Staphylococcus aureus cell wall stress stimulon in response to different cell wall active antibiotics. BMC Microbiol. 2011, 11:16.
    • (2011) BMC Microbiol. , vol.11 , pp. 16
    • Dengler, V.1    Meier, P.S.2    Heusser, R.3    Berger-Bachi, B.4    McCallum, N.5
  • 11
    • 5644229901 scopus 로고    scopus 로고
    • Comparison of two standardisation methods in real-time quantitative RT-PCR to follow Staphylococcus aureus genes expression during in vitro growth
    • Eleaume H., Jabbouri S. Comparison of two standardisation methods in real-time quantitative RT-PCR to follow Staphylococcus aureus genes expression during in vitro growth. J. Microbiol. Methods 2004, 59:363-370.
    • (2004) J. Microbiol. Methods , vol.59 , pp. 363-370
    • Eleaume, H.1    Jabbouri, S.2
  • 12
    • 79960422109 scopus 로고    scopus 로고
    • Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions
    • Ganesh V.K., Barbu E.M., Deivanayagam C.C., et al. Structural and biochemical characterization of Staphylococcus aureus clumping factor B/ligand interactions. J. Biol. Chem. 2011, 286:25963-25972.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25963-25972
    • Ganesh, V.K.1    Barbu, E.M.2    Deivanayagam, C.C.3
  • 14
    • 0033963304 scopus 로고    scopus 로고
    • Direct quantitative transcript analysis of the agr regulon of Staphylococcus aureus during human infection in comparison to the expression profile in vitro
    • Goerke C., Campana S., Bayer M.G., Doring G., Botzenhart K., Wolz C. Direct quantitative transcript analysis of the agr regulon of Staphylococcus aureus during human infection in comparison to the expression profile in vitro. Infect. Immun. 2000, 68:1304-1311.
    • (2000) Infect. Immun. , vol.68 , pp. 1304-1311
    • Goerke, C.1    Campana, S.2    Bayer, M.G.3    Doring, G.4    Botzenhart, K.5    Wolz, C.6
  • 15
    • 3242809005 scopus 로고    scopus 로고
    • An introduction to Staphylococcus aureus, and techniques for identifying and quantifying S. aureus adhesins in relation to adhesion to biomaterials: review
    • Harris L.G., Foster S.J., Richards R.G. An introduction to Staphylococcus aureus, and techniques for identifying and quantifying S. aureus adhesins in relation to adhesion to biomaterials: review. Eur. Cell Mater. 2002, 4:39-60.
    • (2002) Eur. Cell Mater. , vol.4 , pp. 39-60
    • Harris, L.G.1    Foster, S.J.2    Richards, R.G.3
  • 17
    • 79953061200 scopus 로고    scopus 로고
    • Role of Staphylococcus aureus protein A in adherence to silastic catheters
    • Henry-Stanley M.J., Shepherd M.M., Wells C.L., Hess D.J. Role of Staphylococcus aureus protein A in adherence to silastic catheters. J. Surg. Res. 2011, 167:9-13.
    • (2011) J. Surg. Res. , vol.167 , pp. 9-13
    • Henry-Stanley, M.J.1    Shepherd, M.M.2    Wells, C.L.3    Hess, D.J.4
  • 18
    • 0036771636 scopus 로고    scopus 로고
    • SigmaB modulates virulence determinant expression and stress resistance: characterization of a functional rsbU strain derived from Staphylococcus aureus 8325-4
    • Horsburgh M.J., Aish J.L., White I.J., Shaw L., Lithgow J.K., Foster S.J. sigmaB modulates virulence determinant expression and stress resistance: characterization of a functional rsbU strain derived from Staphylococcus aureus 8325-4. J. Bacteriol. 2002, 184:5457-5467.
    • (2002) J. Bacteriol. , vol.184 , pp. 5457-5467
    • Horsburgh, M.J.1    Aish, J.L.2    White, I.J.3    Shaw, L.4    Lithgow, J.K.5    Foster, S.J.6
  • 19
    • 79952302523 scopus 로고    scopus 로고
    • Essential role for the major autolysin in the fibronectin-binding protein-mediated Staphylococcus aureus biofilm phenotype
    • Houston P., Rowe S.E., Pozzi C., Waters E.M., O'Gara J.P. Essential role for the major autolysin in the fibronectin-binding protein-mediated Staphylococcus aureus biofilm phenotype. Infect. Immun. 2011, 79:1153-1165.
    • (2011) Infect. Immun. , vol.79 , pp. 1153-1165
    • Houston, P.1    Rowe, S.E.2    Pozzi, C.3    Waters, E.M.4    O'Gara, J.P.5
  • 20
    • 80053904362 scopus 로고    scopus 로고
    • Identifying protective antigens of Staphylococcus aureus, a pathogen that suppresses host immune responses
    • Kim H.K., Kim H.Y., Schneewind O., Missiakas D. Identifying protective antigens of Staphylococcus aureus, a pathogen that suppresses host immune responses. FASEB J. 2011, 25:3605-3612.
    • (2011) FASEB J. , vol.25 , pp. 3605-3612
    • Kim, H.K.1    Kim, H.Y.2    Schneewind, O.3    Missiakas, D.4
  • 21
    • 0031659829 scopus 로고    scopus 로고
    • Deletion of the alternative sigma factor sigmaB in Staphylococcus aureus reveals its function as a global regulator of virulence genes
    • Kullik I., Giachino P., Fuchs T. Deletion of the alternative sigma factor sigmaB in Staphylococcus aureus reveals its function as a global regulator of virulence genes. J. Bacteriol. 1998, 180:4814-4820.
    • (1998) J. Bacteriol. , vol.180 , pp. 4814-4820
    • Kullik, I.1    Giachino, P.2    Fuchs, T.3
  • 22
    • 0024357241 scopus 로고
    • Reduced adherence to traumatized rat heart valves by a low-fibronectin-binding mutant of Staphylococcus aureus
    • Kuypers J.M., Proctor R.A. Reduced adherence to traumatized rat heart valves by a low-fibronectin-binding mutant of Staphylococcus aureus. Infect. Immun. 1989, 57:2306-2312.
    • (1989) Infect. Immun. , vol.57 , pp. 2306-2312
    • Kuypers, J.M.1    Proctor, R.A.2
  • 23
    • 65449187956 scopus 로고    scopus 로고
    • Capsule expression and genotypic differences among Staphylococcus aureus isolates from patients with chronic or acute osteomyelitis
    • Lattar S.M., Tuchscherr L.P., Caccuri R.L., et al. Capsule expression and genotypic differences among Staphylococcus aureus isolates from patients with chronic or acute osteomyelitis. Infect. Immun. 2009, 77:1968-1975.
    • (2009) Infect. Immun. , vol.77 , pp. 1968-1975
    • Lattar, S.M.1    Tuchscherr, L.P.2    Caccuri, R.L.3
  • 24
    • 33746641280 scopus 로고    scopus 로고
    • Inactivation of a two-component signal transduction system, SaeRS, eliminates adherence and attenuates virulence of Staphylococcus aureus
    • Liang X., Yu C., Sun J., Liu H., Landwehr C., Holmes D., Ji Y. Inactivation of a two-component signal transduction system, SaeRS, eliminates adherence and attenuates virulence of Staphylococcus aureus. Infect. Immun. 2006, 74:4655-4665.
    • (2006) Infect. Immun. , vol.74 , pp. 4655-4665
    • Liang, X.1    Yu, C.2    Sun, J.3    Liu, H.4    Landwehr, C.5    Holmes, D.6    Ji, Y.7
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
    • 66749187185 scopus 로고    scopus 로고
    • Multiple chaperonins in bacteria - why so many?
    • Lund P.A. Multiple chaperonins in bacteria - why so many?. FEMS Microbiol. Rev. 2009, 33:785-800.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 785-800
    • Lund, P.A.1
  • 27
    • 31344439714 scopus 로고    scopus 로고
    • Overexpression of genes of the cell wall stimulon in clinical isolates of Staphylococcus aureus exhibiting vancomycin-intermediate- S. aureus-type resistance to vancomycin
    • McAleese F., Wu S.W., Sieradzki K., Dunman P., Murphy E., Projan S., Tomasz A. Overexpression of genes of the cell wall stimulon in clinical isolates of Staphylococcus aureus exhibiting vancomycin-intermediate- S. aureus-type resistance to vancomycin. J. Bacteriol. 2006, 188:1120-1133.
    • (2006) J. Bacteriol. , vol.188 , pp. 1120-1133
    • McAleese, F.1    Wu, S.W.2    Sieradzki, K.3    Dunman, P.4    Murphy, E.5    Projan, S.6    Tomasz, A.7
  • 28
    • 0031663502 scopus 로고    scopus 로고
    • Role of Staphylococcus aureus surface-associated proteins in the attachment to cultured HaCaT keratinocytes in a new adhesion assay
    • Mempel M., Schmidt T., Weidinger S., Schnopp C., Foster T., Ring J., Abeck D. Role of Staphylococcus aureus surface-associated proteins in the attachment to cultured HaCaT keratinocytes in a new adhesion assay. J. Invest. Dermatol. 1998, 111:452-456.
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 452-456
    • Mempel, M.1    Schmidt, T.2    Weidinger, S.3    Schnopp, C.4    Foster, T.5    Ring, J.6    Abeck, D.7
  • 29
    • 0037945207 scopus 로고    scopus 로고
    • The role of fibronectin binding proteins in the pathogenesis of Staphylococcus aureus infections
    • Menzies B.E. The role of fibronectin binding proteins in the pathogenesis of Staphylococcus aureus infections. Curr. Opin. Infect. Dis. 2003, 16:225-229.
    • (2003) Curr. Opin. Infect. Dis. , vol.16 , pp. 225-229
    • Menzies, B.E.1
  • 30
    • 33748649028 scopus 로고    scopus 로고
    • Global regulatory impact of ClpP protease of Staphylococcus aureus on regulons involved in virulence, oxidative stress response, autolysis, and DNA repair
    • Michel A., Agerer F., Hauck C.R., Herrmann M., Ullrich J., Hacker J., Ohlsen K. Global regulatory impact of ClpP protease of Staphylococcus aureus on regulons involved in virulence, oxidative stress response, autolysis, and DNA repair. J. Bacteriol. 2006, 188:5783-5796.
    • (2006) J. Bacteriol. , vol.188 , pp. 5783-5796
    • Michel, A.1    Agerer, F.2    Hauck, C.R.3    Herrmann, M.4    Ullrich, J.5    Hacker, J.6    Ohlsen, K.7
  • 31
    • 58749108255 scopus 로고    scopus 로고
    • Thermal adaptation of heat shock proteins
    • Muga A., Moro F. Thermal adaptation of heat shock proteins. Curr. Protein Pept. Sci. 2008, 9:552-566.
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 552-566
    • Muga, A.1    Moro, F.2
  • 32
    • 36849071439 scopus 로고    scopus 로고
    • SAMMD: Staphylococcus aureus microarray meta-database
    • Nagarajan V., Elasri M.O. SAMMD: Staphylococcus aureus microarray meta-database. BMC Genomics 2007, 8:351.
    • (2007) BMC Genomics , vol.8 , pp. 351
    • Nagarajan, V.1    Elasri, M.O.2
  • 33
    • 77649273079 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic GrpE protein: insight into thermosensing function for the DnaK chaperone system
    • Nakamura A., Takumi K., Miki K. Crystal structure of a thermophilic GrpE protein: insight into thermosensing function for the DnaK chaperone system. J. Mol. Biol. 2010, 396:1000-1011.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1000-1011
    • Nakamura, A.1    Takumi, K.2    Miki, K.3
  • 34
    • 1642475071 scopus 로고    scopus 로고
    • Staphylococcus aureus capsular polysaccharides
    • O'Riordan K., Lee J.C. Staphylococcus aureus capsular polysaccharides. Clin. Microbiol. Rev. 2004, 17:218-234.
    • (2004) Clin. Microbiol. Rev. , vol.17 , pp. 218-234
    • O'Riordan, K.1    Lee, J.C.2
  • 35
    • 0034462751 scopus 로고    scopus 로고
    • Alternative transcription factor sigma(B) is involved in regulation of biofilm expression in a Staphylococcus aureus mucosal isolate
    • Rachid S., Ohlsen K., Wallner U., Hacker J., Hecker M., Ziebuhr W. Alternative transcription factor sigma(B) is involved in regulation of biofilm expression in a Staphylococcus aureus mucosal isolate. J. Bacteriol. 2000, 182:6824-6826.
    • (2000) J. Bacteriol. , vol.182 , pp. 6824-6826
    • Rachid, S.1    Ohlsen, K.2    Wallner, U.3    Hacker, J.4    Hecker, M.5    Ziebuhr, W.6
  • 36
    • 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., Schumann W. hrcA, the first gene of the Bacillus subtilis dnaK operon encodes a negative regulator of class I heat shock genes. J. Bacteriol. 1996, 178:1088-1093.
    • (1996) J. Bacteriol. , vol.178 , pp. 1088-1093
    • Schulz, A.1    Schumann, W.2
  • 38
    • 54449095003 scopus 로고    scopus 로고
    • Insertional inactivation of branched-chain alpha-keto acid dehydrogenase in Staphylococcus aureus leads to decreased branched-chain membrane fatty acid content and increased susceptibility to certain stresses
    • Singh V.K., Hattangady D.S., Giotis E.S., Singh A.K., Chamberlain N.R., Stuart M.K., Wilkinson B.J. Insertional inactivation of branched-chain alpha-keto acid dehydrogenase in Staphylococcus aureus leads to decreased branched-chain membrane fatty acid content and increased susceptibility to certain stresses. Appl. Environ. Microbiol. 2008, 74:5882-5890.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5882-5890
    • Singh, V.K.1    Hattangady, D.S.2    Giotis, E.S.3    Singh, A.K.4    Chamberlain, N.R.5    Stuart, M.K.6    Wilkinson, B.J.7
  • 39
    • 0142074781 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell-wall-stress stimulon
    • Utaida S., Dunman P.M., Macapagal D., Murphy E., Projan S.J., Singh V.K., Jayaswal R.K., Wilkinson B.J. Genome-wide transcriptional profiling of the response of Staphylococcus aureus to cell-wall-active antibiotics reveals a cell-wall-stress stimulon. Microbiology 2003, 149:2719-2732.
    • (2003) Microbiology , vol.149 , pp. 2719-2732
    • Utaida, S.1    Dunman, P.M.2    Macapagal, D.3    Murphy, E.4    Projan, S.J.5    Singh, V.K.6    Jayaswal, R.K.7    Wilkinson, B.J.8
  • 40
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones - cellular machines for protein folding
    • Walter S., Buchner J. Molecular chaperones - cellular machines for protein folding. Angew. Chem. Int. Ed. Engl. 2002, 41:1098-1113.
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 41
    • 2342507884 scopus 로고    scopus 로고
    • Vancomycin-resistant Staphylococcus aureus in the absence of vancomycin exposure
    • Whitener C.J., Park S.Y., Browne F.A., et al. Vancomycin-resistant Staphylococcus aureus in the absence of vancomycin exposure. Clin. Infect. Dis. 2004, 38:1049-1055.
    • (2004) Clin. Infect. Dis. , vol.38 , pp. 1049-1055
    • Whitener, C.J.1    Park, S.Y.2    Browne, F.A.3


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