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Volumn 148, Issue 10, 2002, Pages 3129-3138

Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays

Author keywords

HrcA; Hsp60; Hsp70; HspR; Transcriptional regulator

Indexed keywords

BACTERIAL ANTIGEN; CRYSTALLIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; SIGMA FACTOR; TRANSCRIPTION FACTOR;

EID: 0036773739     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-148-10-3129     Document Type: Article
Times cited : (301)

References (33)
  • 1
    • 0034113617 scopus 로고    scopus 로고
    • HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine
    • Asea, A., Kraeft, S. K., Kurt-Jones, E. A., Stevenson, M. A., Chen, L. B., Finberg, R. W., Koo, G. C. & Calderwood, S. K. (2000). HSP70 stimulates cytokine production through a CD14-dependent pathway, demonstrating its dual role as a chaperone and cytokine. Nat Med 6, 435-442.
    • (2000) Nat. Med , vol.6 , pp. 435-442
    • Asea, A.1    Kraeft, S.K.2    Kurt-Jones, E.A.3    Stevenson, M.A.4    Chen, L.B.5    Finberg, R.W.6    Koo, G.C.7    Calderwood, S.K.8
  • 2
    • 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. & Smith, C. P. (2000). The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressor. Mol Microbiol 38, 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
  • 3
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways
    • Castellino, F., Boucher, P. E., Eichelberg, K., Mayhew, M., Rothman, J. E., Houghton, A. N. & Germain, R. N. (2000). Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J Exp Med 191, 1957-1964.
    • (2000) J. Exp. Med , vol.191 , pp. 1957-1964
    • Castellino, F.1    Boucher, P.E.2    Eichelberg, K.3    Mayhew, M.4    Rothman, J.E.5    Houghton, A.N.6    Germain, R.N.7
  • 4
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang, Z., Primm, T. P., Jakana, J., Lee, I. H., Serysheva, I., Chiu, W., Gilbert, H. F. & Quiocho, F. A. (1996). Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J Biol Chem 271, 7218-7223.
    • (1996) J. Biol. Chem , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 5
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • & 39 other authors
    • Cole, S. T., Brosch, R., Parkhill, J. & 39 other authors (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 6
    • 0031930142 scopus 로고    scopus 로고
    • Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton α-crystallin homolog
    • Cunningham, A. F. & Spreadbury, C. L. (1998). Mycobacterial stationary phase induced by low oxygen tension: cell wall thickening and localization of the 16-kilodalton α-crystallin homolog. J Bacteriol 180, 801-808.
    • (1998) J. Bacteriol , vol.180 , pp. 801-808
    • Cunningham, A.F.1    Spreadbury, C.L.2
  • 7
    • 0032779309 scopus 로고    scopus 로고
    • A mycobacterial extracytoplasmic sigma factor involved in survival following heat shock and oxidative stress
    • Fernandes, N. D., Wu, Q. L., Kong, D., Puyang, X., Garg, S. & Husson, R. N. (1999). A mycobacterial extracytoplasmic sigma factor involved in survival following heat shock and oxidative stress. J Bacteriol 181, 4266-4274.
    • (1999) J. Bacteriol , vol.181 , pp. 4266-4274
    • Fernandes, N.D.1    Wu, Q.L.2    Kong, D.3    Puyang, X.4    Garg, S.5    Husson, R.N.6
  • 8
    • 0032958502 scopus 로고    scopus 로고
    • The ClpB ATPase of Streptomyces albus G belongs to the HspR heat shock regulon
    • Grandvalet, C., de Crecy-Lagard, V. & Mazodier, P. (1999). The ClpB ATPase of Streptomyces albus G belongs to the HspR heat shock regulon. Mol Microbiol 31, 521-532.
    • (1999) Mol. Microbiol , vol.31 , pp. 521-532
    • Grandvalet, C.1    de Crecy-Lagard, V.2    Mazodier, P.3
  • 9
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heat-shock promoters
    • Grossman, A. D., Erickson, J. W. & Gross, C. A. (1984). The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell 38, 383-390.
    • (1984) Cell , vol.38 , pp. 383-390
    • Grossman, A.D.1    Erickson, J.W.2    Gross, C.A.3
  • 10
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 11
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker, M., Schumann, W. & Volker, U. (1996). Heat-shock and general stress response in Bacillus subtilis. Mol Microbiol 19, 417-428.
    • (1996) Mol. Microbiol , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Volker, U.3
  • 14
    • 0029091479 scopus 로고
    • Identification of macrophage and stress-induced proteins of Mycobacterium tuberculosis
    • Lee, B. Y. & Horwitz, M. A. (1995). Identification of macrophage and stress-induced proteins of Mycobacterium tuberculosis. J Clin Invest 96, 245-249.
    • (1995) J. Clin. Invest , vol.96 , pp. 245-249
    • Lee, B.Y.1    Horwitz, M.A.2
  • 15
    • 0032955397 scopus 로고    scopus 로고
    • Differential expression of 10 sigma factor genes in Mycobacterium tuberculosis
    • Manganelli, R., Dubnau, E., Tyagi, S., Kramer, F. R. & Smith, I. (1999). Differential expression of 10 sigma factor genes in Mycobacterium tuberculosis. Mol Microbiol 31, 715-724.
    • (1999) Mol. Microbiol , vol.31 , pp. 715-724
    • Manganelli, R.1    Dubnau, E.2    Tyagi, S.3    Kramer, F.R.4    Smith, I.5
  • 17
    • 0035133932 scopus 로고    scopus 로고
    • Differential expression of mycobacterial proteins following phagocytosis by macrophages
    • Monahan, I., Betts, J., Banerjee, D. & Butcher, P. (2001). Differential expression of mycobacterial proteins following phagocytosis by macrophages. Microbiology 147, 459-471.
    • (2001) Microbiology , vol.147 , pp. 459-471
    • Monahan, I.1    Betts, J.2    Banerjee, D.3    Butcher, P.4
  • 18
    • 0032944541 scopus 로고    scopus 로고
    • Negative regulation of bacterial heat shock genes
    • Narberhaus, F. (1999). Negative regulation of bacterial heat shock genes. Mol Microbiol 31, 1-8.
    • (1999) Mol. Microbiol , vol.31 , pp. 1-8
    • Narberhaus, F.1
  • 19
    • 0030884810 scopus 로고    scopus 로고
    • Development and use of a conditional antisense mutagenesis system in mycobacteria
    • Parish, T. & Stoker, N.G. (1997). Development and use of a conditional antisense mutagenesis system in mycobacteria. FEMS Microbiol Lett 154, 151-157.
    • (1997) FEMS Microbiol. Lett , vol.154 , pp. 151-157
    • Parish, T.1    Stoker, N.G.2
  • 20
    • 0026325351 scopus 로고
    • Characterization of the heat shock response in Mycobacterium bovis BCG
    • Patel, B. K., Banerjee, D. K. & Butcher, P. D. (1991). Characterization of the heat shock response in Mycobacterium bovis BCG. J Bacteriol 173, 7982-7987.
    • (1991) J. Bacteriol , vol.173 , pp. 7982-7987
    • Patel, B.K.1    Banerjee, D.K.2    Butcher, P.D.3
  • 21
    • 0034805644 scopus 로고    scopus 로고
    • The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis
    • Raman, S., Song, T., Puyang, X., Bardarov, S., Jacobs, W. R., Jr & Husson, R. N. (2001). The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. J Bacteriol 183, 6119-6125.
    • (2001) J. Bacteriol , vol.183 , pp. 6119-6125
    • Raman, S.1    Song, T.2    Puyang, X.3    Bardarov, S.4    Jacobs W.R., Jr.5    Husson, R.N.6
  • 23
    • 0034948578 scopus 로고    scopus 로고
    • Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection
    • & 7 other authors
    • Stewart, G. R., Snewin, V. A., Walzi, G. & 7 other authors (2001). Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection. Nat Med 7, 732-737.
    • (2001) Nat. Med , vol.7 , pp. 732-737
    • Stewart, G.R.1    Snewin, V.A.2    Walzi, G.3
  • 25
    • 0026539069 scopus 로고
    • Tuberculosis: A global overview of the situation today
    • Sudre, P., ten Dam, G. & Kochi, A. (1992). Tuberculosis: a global overview of the situation today. Bull W H O 70, 149-159.
    • (1992) Bull. W H O , vol.70 , pp. 149-159
    • Sudre, P.1    ten Dam, G.2    Kochi, A.3
  • 26
    • 0028979675 scopus 로고
    • A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides
    • Suto, R. & Srivastava, P. K. (1995). A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269, 1585-1588.
    • (1995) Science , vol.269 , pp. 1585-1588
    • Suto, R.1    Srivastava, P.K.2
  • 27
    • 0030589083 scopus 로고    scopus 로고
    • Electroporation at elevated temperatures substantially improves transformation efficiency of slow-growing mycobacteria
    • Wards, B. J. & Collins, D. M. (1996). Electroporation at elevated temperatures substantially improves transformation efficiency of slow-growing mycobacteria. FEMS Microbiol Lett 145, 101-105.
    • (1996) FEMS Microbiol. Lett , vol.145 , pp. 101-105
    • Wards, B.J.1    Collins, D.M.2
  • 29
    • 0000942354 scopus 로고    scopus 로고
    • Functional genomics of Mycobacterium tuberculosis using DNA microarrays
    • Mycobacterium tuberculosis Protocols, Edited by T. Parish & N. G. Stoker. Totowa, NJ: Humana Press
    • Wilson, M., Voskuil, M., Schnappinger, D. & Schoolnik, G. K. (2001). Functional genomics of Mycobacterium tuberculosis using DNA microarrays. In Methods in Molecular Medicine, vol. 54: Mycobacterium tuberculosis Protocols, pp. 335-357. Edited by T. Parish & N. G. Stoker. Totowa, NJ: Humana Press.
    • (2001) Methods in Molecular Medicine , vol.54 , pp. 335-357
    • Wilson, M.1    Voskuil, M.2    Schnappinger, D.3    Schoolnik, G.K.4
  • 30
    • 0032898210 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity
    • Yang, H., Huang, S., Dai, H., Gong, Y., Zheng, C. & Chang, Z. (1999). The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity. Protein Sci 8, 174-179.
    • (1999) Protein Sci , vol.8 , pp. 174-179
    • Yang, H.1    Huang, S.2    Dai, H.3    Gong, Y.4    Zheng, C.5    Chang, Z.6
  • 31
    • 0025776531 scopus 로고
    • Heat shock proteins and antigens of Mycobacterium tuberculosis
    • Young, D. B. & Garbe, T. R. (1991). Heat shock proteins and antigens of Mycobacterium tuberculosis. Infect Immun 59, 3086-3093.
    • (1991) Infect. Immun , vol.59 , pp. 3086-3093
    • Young, D.B.1    Garbe, T.R.2
  • 32
    • 0029785912 scopus 로고    scopus 로고
    • Stationary phase-associated protein expression in Mycobacterium tuberculosis: Function of the mycobacterial α-crystallin homolog
    • Yuan, Y., Crane, D. D. & Barry, C. E., 3rd (1996). Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial α-crystallin homolog. J Bacteriol 178, 4484-4492.
    • (1996) J. Bacteriol , vol.178 , pp. 4484-4492
    • Yuan, Y.1    Crane, D.D.2    Barry C.E. III3


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