메뉴 건너뛰기




Volumn 150, Issue 7, 2004, Pages 2135-2141

Autophosphorylation of the 16 kDa and 70 kDa antigens (Hsp 16.3 and Hsp 70) of Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; CALCIUM ION; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 16 3; HEAT SHOCK PROTEIN 70; MYCOBACTERIUM ANTIGEN; PHOSPHOAMINO ACID; PROTEIN DNAK; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 4344667325     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26789-0     Document Type: Article
Times cited : (15)

References (40)
  • 1
    • 0032728879 scopus 로고    scopus 로고
    • Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB
    • Av-Gay, Y., Jamil, S. & Drews, S. J. (1999). Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB. Infect Immun 67, 5676-5682.
    • (1999) Infect. Immun. , vol.67 , pp. 5676-5682
    • Av-Gay, Y.1    Jamil, S.2    Drews, S.J.3
  • 2
    • 0036183002 scopus 로고    scopus 로고
    • Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division
    • Chaba, R., Raje, M. & Chakraborti, P. K. (2002). Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division. Eur J Biochem 269, 1078-1085.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1078-1085
    • Chaba, R.1    Raje, M.2    Chakraborti, P.K.3
  • 3
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) 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 (Hsp 16.3) 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
  • 4
    • 0027962609 scopus 로고
    • Protein tyrosine phosphorylation in Mycobacterium tuberculosis
    • Chow, K., Ng, D., Stokes, R. & Johnson, P. (1994). Protein tyrosine phosphorylation in Mycobacterium tuberculosis. FEMS Microbiol Lett 124, 203-207.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 203-207
    • Chow, K.1    Ng, D.2    Stokes, R.3    Johnson, P.4
  • 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
    • 0032605255 scopus 로고    scopus 로고
    • Identification of proteins by matrix-assisted laser desorption/ionization mass spectrometry using peptide and fragment ion masses
    • Courchesne, P. L. & Patterson, S. D. (1999). Identification of proteins by matrix-assisted laser desorption/ionization mass spectrometry using peptide and fragment ion masses. Methods Mol Biol 112, 487-511.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 487-511
    • Courchesne, P.L.1    Patterson, S.D.2
  • 7
    • 0027511372 scopus 로고
    • ATP-dependent protein kinases in bacteria
    • Cozzone, A. J. (1993). ATP-dependent protein kinases in bacteria. J Cell Biochem 51, 7-13.
    • (1993) J. Cell Biochem. , vol.51 , pp. 7-13
    • Cozzone, A.J.1
  • 8
    • 0027471981 scopus 로고
    • Immunopathogenesis of pulmonary tuberculosis
    • Dannenberg, A. M., Jr (1993). Immunopathogenesis of pulmonary tuberculosis. Hosp Pract (Off Ed) 28, 51-58.
    • (1993) Hosp. Pract. (Off Ed.) , vol.28 , pp. 51-58
    • Dannenberg Jr., A.M.1
  • 9
    • 0035910174 scopus 로고    scopus 로고
    • A protein kinase inhibitor as an antimycobacterial agent
    • Drews, S. J., Hung, F. & Av-Gay, Y. (2001). A protein kinase inhibitor as an antimycobacterial agent. FEMS Microbiol Lett 205, 369-374.
    • (2001) FEMS Microbiol. Lett. , vol.205 , pp. 369-374
    • Drews, S.J.1    Hung, F.2    Av-Gay, Y.3
  • 10
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos, B., Marcandier, S. & Cozzone, A. J. (1991). Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol 201, 10-21.
    • (1991) Methods Enzymol. , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.J.3
  • 11
    • 0028023344 scopus 로고
    • Structure and modifications of the junior chaperone alpha-crystallin From lens transparency to molecular pathology
    • Groenen, P. J., Merck, K. B., de Jong, W. W. & Bloemendal, H. (1994). Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur J Biochem 225, 1-19.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 1-19
    • Groenen, P.J.1    Merck, K.B.2    de Jong, W.W.3    Bloemendal, H.4
  • 12
    • 0033118181 scopus 로고    scopus 로고
    • In vitro evidence of two-component system phosphorylation between the Mycobacterium tuberculosis TrcR/TrcS proteins
    • Haydel, S. E., Dunlap, N. E. & Benjamin, W. H., Jr (1999). In vitro evidence of two-component system phosphorylation between the Mycobacterium tuberculosis TrcR/TrcS proteins. Microb Pathog 26, 195-206.
    • (1999) Microb. Pathog. , vol.26 , pp. 195-206
    • Haydel, S.E.1    Dunlap, N.E.2    Benjamin Jr., W.H.3
  • 13
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: Protein quality control and regulatory principles
    • Hengge, R. & Bukau, B. (2003). Proteolysis in prokaryotes: protein quality control and regulatory principles. Mol Microbiol 49, 1451-1462.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 14
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz, J. (1992). Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A 89, 10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 15
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. (1995). Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 16
    • 0028346451 scopus 로고
    • Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • Kato, K., Hasegawa, K., Goto, S. & Inaguma, Y. (1994). Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem 269, 11274-11278.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 17
    • 0033806882 scopus 로고    scopus 로고
    • Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
    • Koul, A., Choidas, A., Treder, M., Tyagi, A. K., Drlica, K., Singh, Y. & Ullrich, A. (2000). Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis. J Bacteriol 182, 5425-5432.
    • (2000) J. Bacteriol. , vol.182 , pp. 5425-5432
    • Koul, A.1    Choidas, A.2    Treder, M.3    Tyagi, A.K.4    Drlica, K.5    Singh, Y.6    Ullrich, A.7
  • 18
    • 0034873897 scopus 로고    scopus 로고
    • Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: Characterization and localization
    • Koul, A., Choidas, A., Tyagi, A. K., Drlica, K., Singh, Y. & Ullrich, A. (2001). Serine/threonine protein kinases PknF and PknG of Mycobacterium tuberculosis: characterization and localization. Microbiology 147, 2307-2314.
    • (2001) Microbiology , vol.147 , pp. 2307-2314
    • Koul, A.1    Choidas, A.2    Tyagi, A.K.3    Drlica, K.4    Singh, Y.5    Ullrich, A.6
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0025310526 scopus 로고
    • Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region
    • Matsuyama, S., Kimura, E. & Mizushima, S. (1990). Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region. J Biol Chem 265, 8760-8765.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8760-8765
    • Matsuyama, S.1    Kimura, E.2    Mizushima, S.3
  • 21
    • 0037018884 scopus 로고    scopus 로고
    • Molecular analysis of the dormancy response in Mycobacterium smegmatis: Expression analysis of genes encoding the DevR-DevS two-component system, Rv3134c and chaperone alpha-crystallin homologues
    • Mayuri, Bagchi, G., Das, T. K. & Tyagi, J. S. (2002). Molecular analysis of the dormancy response in Mycobacterium smegmatis: expression analysis of genes encoding the DevR-DevS two-component system, Rv3134c and chaperone alpha-crystallin homologues. FEMS Microbiol Lett 211, 231-237.
    • (2002) FEMS Microbiol. Lett. , vol.211 , pp. 231-237
    • Mayuri, A.1    Bagchi, G.2    Das, T.K.3    Tyagi, J.S.4
  • 22
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty, J. S. & Walker, G. C. (1991). DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc Natl Acad Sci U S A 88, 9513-9517.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 23
    • 0023696905 scopus 로고
    • The inhibitory effects of mycobacterial lipoarabinomannan and polysaccharides upon polyclonal and monoclonal human T cell proliferation
    • Moreno, C., Mehlert, A. & Lamb, J. (1988). The inhibitory effects of mycobacterial lipoarabinomannan and polysaccharides upon polyclonal and monoclonal human T cell proliferation. Clin Exp Immunol 74, 206-210.
    • (1988) Clin. Exp. Immunol. , vol.74 , pp. 206-210
    • Moreno, C.1    Mehlert, A.2    Lamb, J.3
  • 24
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau, K., Das, A. & Walsh, C. T. (1993). Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J Biol Chem 268, 1479-1487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 25
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P. Z., Goodman, H. M. & O'Farrell, P. H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12, 1133-1141.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 26
    • 0037460102 scopus 로고    scopus 로고
    • A novel TB vaccine; Strategies to combat a complex pathogen
    • Olsen, A. W. & Andersen, P. (2003). A novel TB vaccine; strategies to combat a complex pathogen. Immunol Lett 85, 207-211.
    • (2003) Immunol. Lett. , vol.85 , pp. 207-211
    • Olsen, A.W.1    Andersen, P.2
  • 27
    • 0037373063 scopus 로고    scopus 로고
    • A two-component regulator of universal stress protein expression and adaptation to oxygen starvation in Mycobacterium smegmatis
    • O'Toole, R., Smeulders, M. J., Blokpoel, M. C., Kay, E. J., Lougheed, K. & Williams, H. D. (2003). A two-component regulator of universal stress protein expression and adaptation to oxygen starvation in Mycobacterium smegmatis. J Bacteriol 185, 1543-1554.
    • (2003) J. Bacteriol. , vol.185 , pp. 1543-1554
    • O'Toole, R.1    Smeulders, M.J.2    Blokpoel, M.C.3    Kay, E.J.4    Lougheed, K.5    Williams, H.D.6
  • 28
    • 0032497336 scopus 로고    scopus 로고
    • Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics
    • Peake, P., Winter, N. & Britton, W. (1998). Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics. Biochim Biophys Acta 1387, 387-394.
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 387-394
    • Peake, P.1    Winter, N.2    Britton, W.3
  • 29
    • 0031039634 scopus 로고    scopus 로고
    • A serine/threonine protein kinase from Mycobacterium tuberculosis
    • Peirs, P., De Wit, L., Braibant, M., Huygen, K. & Content, J. (1997). A serine/threonine protein kinase from Mycobacterium tuberculosis. Eur J Biochem 244, 604-612.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 604-612
    • Peirs, P.1    De Wit, L.2    Braibant, M.3    Huygen, K.4    Content, J.5
  • 30
    • 0034067933 scopus 로고    scopus 로고
    • Regulation by protein kinase of phagocytosis of Mycobacterium leprae by macrophages
    • Prabhakaran, K., Harris, E. B. & Randhawa, B. (2000). Regulation by protein kinase of phagocytosis of Mycobacterium leprae by macrophages. J Med Microbiol 49, 339-342.
    • (2000) J. Med. Microbiol. , vol.49 , pp. 339-342
    • Prabhakaran, K.1    Harris, E.B.2    Randhawa, B.3
  • 31
    • 0028245134 scopus 로고
    • Identification of a Mycobacterium leprae-specific T cell epitope on the 70 kDa heat shock protein
    • Roche, P. W., Peake, P. W., Davenport, M. P. & Britton, W. J. (1994). Identification of a Mycobacterium leprae-specific T cell epitope on the 70 kDa heat shock protein. Immunol Cell Biol 72, 215-221.
    • (1994) Immunol. Cell Biol. , vol.72 , pp. 215-221
    • Roche, P.W.1    Peake, P.W.2    Davenport, M.P.3    Britton, W.J.4
  • 33
    • 0031593689 scopus 로고    scopus 로고
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607. Mol Cell Biochem 183, 183-191.
    • (1996) Mol. Cell Biochem. , vol.183 , pp. 183-191
    • Sharma, S.1    Giri, S.2    Khuller, G.K.3
  • 34
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins on silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. (1996). Mass spectrometric sequencing of proteins on silver-stained polyacrylamide gels. Anal Chem 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 35
    • 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 World Health Organ 70, 149-159.
    • (1992) Bull. World Health Organ. , vol.70 , pp. 149-159
    • Sudre, P.1    ten Dam, G.2    Kochi, A.3
  • 36
    • 85047698890 scopus 로고    scopus 로고
    • Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallin
    • Valdez, M. M., Clark, J. I., Wu, G. J. & Muchowski, P. J. (2002). Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallin. Eur J Biochem 269, 1806-1813.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1806-1813
    • Valdez, M.M.1    Clark, J.I.2    Wu, G.J.3    Muchowski, P.J.4
  • 37
    • 0026527770 scopus 로고
    • The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins
    • Verbon, A., Hartskeerl, R. A., Schuitema, A., Kolk, A. H., Young, D. B. & Lathigra, R. (1992). The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins. J Bacteriol 174, 1352-1359.
    • (1992) J. Bacteriol. , vol.174 , pp. 1352-1359
    • Verbon, A.1    Hartskeerl, R.A.2    Schuitema, A.3    Kolk, A.H.4    Young, D.B.5    Lathigra, R.6
  • 38
    • 0028603583 scopus 로고
    • Dormancy of Mycobacterium tuberculosis and latency of disease
    • Wayne, L. G. (1994). Dormancy of Mycobacterium tuberculosis and latency of disease. Eur J Clin Microbiol Infect Dis 13, 908-914.
    • (1994) Eur. J. Clin. Microbiol. Infect. Dis. , vol.13 , pp. 908-914
    • Wayne, L.G.1
  • 39
    • 0029785912 scopus 로고    scopus 로고
    • Stationary phase-associated protein expression in Mycobacterium tuberculosis: Function of the mycobacterial alpha-crystallin homolog
    • Yuan, Y., Crane, D. D. & Barry, C. E., 3rd (1996). Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial alpha-crystallin homolog. J Bacteriol 178, 4484-4492.
    • (1996) J. Bacteriol. , vol.178 , pp. 4484-4492
    • Yuan, Y.1    Crane, D.D.2    Barry III, C.E.3
  • 40
    • 0043104253 scopus 로고
    • The DnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system
    • Zylicz, M., LeBowitz, J. H., McMacken, R. & Georgopoulos, C. (1983). The DnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc Natl Acad Sci U S A 80, 6431-6435.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 6431-6435
    • Zylicz, M.1    LeBowitz, J.H.2    McMacken, R.3    Georgopoulos, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.