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Volumn 181, Issue 5, 1999, Pages 1380-1387

Transcription of the stationary-phase-associated hspX gene of Mycobacterium tuberculosis is inversely related to synthesis of the 16- kilodalton protein

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Indexed keywords

ALPHA CRYSTALLIN;

EID: 0033018002     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.5.1380-1387.1999     Document Type: Article
Times cited : (52)

References (42)
  • 1
    • 0024834348 scopus 로고
    • Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene
    • Aldea, M., T. Garrido, C. Hernández-Chico, M. Vicente, and S. R. Kushner. 1989. Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene. EMBO J. 8:3923-3931.
    • (1989) EMBO J. , vol.8 , pp. 3923-3931
    • Aldea, M.1    Garrido, T.2    Hernández-Chico, C.3    Vicente, M.4    Kushner, S.R.5
  • 2
    • 0025173687 scopus 로고
    • Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters
    • Aldea, M., T. Garrido, J. Pla, and M. Vicente. 1990. Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters. EMBO J. 9:3787-3794.
    • (1990) EMBO J. , vol.9 , pp. 3787-3794
    • Aldea, M.1    Garrido, T.2    Pla, J.3    Vicente, M.4
  • 3
    • 0029747225 scopus 로고    scopus 로고
    • A study of the mycobacterial transcriptional apparatus: Identification of novel features in promoter elements
    • Bashyam, M. D., D. Kaushal, S. K. Dasgupta, and A. K. Tyagi. 1996. A study of the mycobacterial transcriptional apparatus: identification of novel features in promoter elements. J. Bacteriol. 178:4847-4853.
    • (1996) J. Bacteriol. , vol.178 , pp. 4847-4853
    • Bashyam, M.D.1    Kaushal, D.2    Dasgupta, S.K.3    Tyagi, A.K.4
  • 5
    • 0028903455 scopus 로고
    • The expanding small heat shock family, and structure predictions of the conserved "α-crystallin domain."
    • Caspers, G.-J., J. A. M. Leunissen, and W. W. de Jong. 1995. The expanding small heat shock family, and structure predictions of the conserved "α-crystallin domain." J. Mol. Evol. 40:238-248.
    • (1995) J. Mol. Evol. , vol.40 , pp. 238-248
    • Caspers, G.-J.1    Leunissen, J.A.M.2    De Jong, W.W.3
  • 6
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang, Z., T. P. Primm, J. Jakana, I. H. Lee, I. Serysheva, W. Chiu, H. F. Gilbart, and F. A. Quiocho. 1996. Mycobacterium tuberculosis 16kDa 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    Gilbart, H.F.7    Quiocho, F.A.8
  • 7
    • 0019408242 scopus 로고
    • Antigenic diversity of Mycobacterium tuberculosis and Mycobacterium bovis detected by means of monoclonal antibodies
    • Coates, A. R. M., J. Hewitt, B. W. Allen, J. Ivanyi, and D. A. Mitchison. 1981. Antigenic diversity of Mycobacterium tuberculosis and Mycobacterium bovis detected by means of monoclonal antibodies. Lancet ii:167-169.
    • (1981) Lancet , vol.2 , pp. 167-169
    • Coates, A.R.M.1    Hewitt, J.2    Allen, B.W.3    Ivanyi, J.4    Mitchison, D.A.5
  • 9
    • 0015500979 scopus 로고
    • Regulation of ribosomal and transfer RNA synthesis in Escherichia coli B/r
    • Dennis, P. P. 1972. Regulation of ribosomal and transfer RNA synthesis in Escherichia coli B/r. J. Biol. Chem. 247:2842-2845.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2842-2845
    • Dennis, P.P.1
  • 10
    • 0019486287 scopus 로고
    • Experimental models to explain the high sterilizing activity of rifampin in the chemotherapy of tuberculosis
    • Dickinson, J. M., and D. A. Mitchison. 1981. Experimental models to explain the high sterilizing activity of rifampin in the chemotherapy of tuberculosis. Am. Rev. Respir. Dis. 123:367-371.
    • (1981) Am. Rev. Respir. Dis. , vol.123 , pp. 367-371
    • Dickinson, J.M.1    Mitchison, D.A.2
  • 11
    • 0023886015 scopus 로고
    • Posttranscriptional regulation mechanisms in Escherichia coli
    • Gold, L. 1988. Posttranscriptional regulation mechanisms in Escherichia coli. Ann. Rev. Biochem. 57:199-233.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 199-233
    • Gold, L.1
  • 12
    • 0030669069 scopus 로고    scopus 로고
    • Role of Escherichia coli cspA promoter sequences and adaptation of translational apparatus in the cold shock response
    • Goldenberg, D., I. Azar, A. B. Oppenheim, A. Brandi, C. L. Pon, and C. O. Gualerzi. 1997. Role of Escherichia coli cspA promoter sequences and adaptation of translational apparatus in the cold shock response. Mol. Gen. Genet. 256:282-290.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 282-290
    • Goldenberg, D.1    Azar, I.2    Oppenheim, A.B.3    Brandi, A.4    Pon, C.L.5    Gualerzi, C.O.6
  • 13
    • 0022475085 scopus 로고
    • DNA determinants of rRNA synthesis in E. coli: Growth rate dependent regulation, feedback inhibition, upstream activation, anti-termination
    • Gourse, R. L., H. A. de Boer, and M. Normura. 1986 DNA determinants of rRNA synthesis in E. coli: growth rate dependent regulation, feedback inhibition, upstream activation, anti-termination. Cell 44:197-205.
    • (1986) Cell , vol.44 , pp. 197-205
    • Gourse, R.L.1    De Boer, H.A.2    Normura, M.3
  • 14
    • 0026483279 scopus 로고
    • α-Crystallin can act as a molecular chaperone
    • Horwitz, J. 1992. α-Crystallin can act as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 15
    • 0031912339 scopus 로고    scopus 로고
    • Protein synthesis is shutdown in dormant Mycobacterium tuberculosis and is reversed by oxygen or heat shock
    • Hu, Y. M., P. D. Butcher, K. Sole, D. A. Mitchison, and A. R. M. Coates. 1998. Protein synthesis is shutdown in dormant Mycobacterium tuberculosis and is reversed by oxygen or heat shock. FEMS Microbiol. Lett. 158:139-145.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 139-145
    • Hu, Y.M.1    Butcher, P.D.2    Sole, K.3    Mitchison, D.A.4    Coates, A.R.M.5
  • 16
    • 0018876711 scopus 로고
    • Secondary structure of mRNA and efficiency of translation initiation
    • Iserentant, D., and W. Fiers. 1980. Secondary structure of mRNA and efficiency of translation initiation. Gene 9:1-12.
    • (1980) Gene , vol.9 , pp. 1-12
    • Iserentant, D.1    Fiers, W.2
  • 17
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., M. Gaestel, K. Engel, and J. Buchner. 1992. Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268:1517-1520.
    • (1992) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 18
    • 0026026102 scopus 로고
    • The global tuberculosis situation and the new control strategy of the World Health Organization
    • Kochi, A. 1991. The global tuberculosis situation and the new control strategy of the World Health Organization. Tubercle 72:1-6.
    • (1991) Tubercle , vol.72 , pp. 1-6
    • Kochi, A.1
  • 19
    • 0028176450 scopus 로고
    • s subunit of RNA-polymerase in Escherichia coli is controlled at the levels of transcription, translation and protein stability
    • s subunit of RNA-polymerase in Escherichia coli is controlled at the levels of transcription, translation and protein stability. Genes Dev. 8:1600-1612.
    • (1994) Genes Dev. , vol.8 , pp. 1600-1612
    • Lange, R.1    Hengge-Aronis, R.2
  • 20
    • 0025727532 scopus 로고
    • Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells
    • Langry, J., P. Chrétien, A. Laszlo, and H. Lambert. 1991. Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells. J. Cell. Physiol. 147:93-101.
    • (1991) J. Cell. Physiol. , vol.147 , pp. 93-101
    • Langry, J.1    Chrétien, P.2    Laszlo, A.3    Lambert, H.4
  • 22
    • 0023046899 scopus 로고
    • Secondary structure as primary determination of the efficiency of ribosomal binding sites in Escherichia coli
    • Looman A. C., J. Bodlaender, M. de Gruyter, A. Vogelaar, and P. H. van Knippenberg. 1986. Secondary structure as primary determination of the efficiency of ribosomal binding sites in Escherichia coli. Nucleic Acids Res. 14:5481-5497.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5481-5497
    • Looman A, C.1    Bodlaender, J.2    De Gruyter, M.3    Vogelaar, A.4    Van Knippenberg, P.H.5
  • 23
    • 0025166089 scopus 로고
    • Secondary structure of the ribosome binding site determines translational efficiency: A quantitative analysis
    • Maarten, H. de Smit, and J. van Duin. 1990. Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis. Proc. Natl. Acad. Sci. USA 87:7668-7672.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7668-7672
    • De Maarten, H.S.1    Van Duin, J.2
  • 24
    • 0030835641 scopus 로고    scopus 로고
    • An effective method of RNA extraction from bacteria refractory to disruption, including mycobacteria
    • Mangan, J. A., K. M. Sole, D. A. Mitchison, and P. D. Butcher. 1997. An effective method of RNA extraction from bacteria refractory to disruption, including mycobacteria. Nucleic Acids Res. 25:675-676.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 675-676
    • Mangan, J.A.1    Sole, K.M.2    Mitchison, D.A.3    Butcher, P.D.4
  • 25
    • 0025978756 scopus 로고
    • The molecular basis of carbon-starvation-induced general resistance in Escherichia coli
    • Matin, A. 1991. The molecular basis of carbon-starvation-induced general resistance in Escherichia coli. Mol. Microbiol. 5:3-10.
    • (1991) Mol. Microbiol. , vol.5 , pp. 3-10
    • Matin, A.1
  • 26
    • 0027412046 scopus 로고
    • The putative σ factor KatF is regulated posttranscriptionally during carbon starvation
    • McCann, M. P., C. D. Fraley, and A Matin. 1993. The putative σ factor KatF is regulated posttranscriptionally during carbon starvation. J. Bacteriol. 175: 2143-2149.
    • (1993) J. Bacteriol. , vol.175 , pp. 2143-2149
    • McCann, M.P.1    Fraley, C.D.2    Matin, A.3
  • 27
    • 0024440105 scopus 로고
    • Biochemical and antigenic characterization of the Mycobacterium tuberculosis 71 kD antigen, a member of the 70 kD heat-shock protein family
    • Mehlert, A., and D. B. Young. 1989. Biochemical and antigenic characterization of the Mycobacterium tuberculosis 71 kD antigen, a member of the 70 kD heat-shock protein family. Mol. Microbiol. 3:125-130.
    • (1989) Mol. Microbiol. , vol.3 , pp. 125-130
    • Mehlert, A.1    Young, D.B.2
  • 28
    • 0024524730 scopus 로고
    • Transcriptional and posttranscriptional control of the Bacillus subtilis succinate dehydrogenase operon
    • Melin, L., L. Rutberg, and A. von Gabain. 1989. Transcriptional and posttranscriptional control of the Bacillus subtilis succinate dehydrogenase operon. J. Bacteriol. 171:2110-2115.
    • (1989) J. Bacteriol. , vol.171 , pp. 2110-2115
    • Melin, L.1    Rutberg, L.2    Von Gabain, A.3
  • 29
    • 0024117856 scopus 로고
    • Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E
    • Mudd, E. A., P. Prentki, D. Belin, and H. M. Krisch. 1988. Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E. EMBO J. 7:3601-3607.
    • (1988) EMBO J. , vol.7 , pp. 3601-3607
    • Mudd, E.A.1    Prentki, P.2    Belin, D.3    Krisch, H.M.4
  • 30
    • 0021202461 scopus 로고
    • Growth-rate dependent regulation of mRNA stability in Escherichia coli
    • Nilsson, G., J. G. Belasco, S. N. Cohen, and A. Von Gabain. 1984 Growth-rate dependent regulation of mRNA stability in Escherichia coli. Nature (London) 312:75-77.
    • (1984) Nature (London) , vol.312 , pp. 75-77
    • Nilsson, G.1    Belasco, J.G.2    Cohen, S.N.3    Von Gabain, A.4
  • 31
    • 0025166244 scopus 로고
    • Changes in the stability of specific mRNA species in response to growth stage in Bacillus subtilis
    • Resnekov, O., L. Butberg, and A. von Gabain. 1990. Changes in the stability of specific mRNA species in response to growth stage in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 87:8355-8359.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8355-8359
    • Resnekov, O.1    Butberg, L.2    Von Gabain, A.3
  • 34
    • 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., R. A. Hartskeerl, A. Schuitema, A. H. Kolk, D. B. Young, and R. Lathigra. 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
  • 35
    • 0025769253 scopus 로고
    • The role of the 'gearbox' in the transcription of essential genes
    • Vicente, M., S. R. Kushner, T. Garrido, and M. Aldea. 1991. The role of the 'gearbox' in the transcription of essential genes. Mol. Microbiol. 5:2085-2091.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2085-2091
    • Vicente, M.1    Kushner, S.R.2    Garrido, T.3    Aldea, M.4
  • 36
    • 0025787736 scopus 로고
    • Micellar subunit assembly in a three-layer model of oliomeric α-crystallin
    • Walsh, M. T., A. C. Sen, and B. Chakrabarti. 1991. Micellar subunit assembly in a three-layer model of oliomeric α-crystallin. J. Biol. Them. 266:20079-20084.
    • (1991) J. Biol. Them. , vol.266 , pp. 20079-20084
    • Walsh, M.T.1    Sen, A.C.2    Chakrabarti, B.3
  • 37
    • 0017107790 scopus 로고
    • Dynamics of submerged growth of Mycobacterium tuberculosis under aerobic and microaerophilic conditions
    • Wayne, L. G. 1976. Dynamics of submerged growth of Mycobacterium tuberculosis under aerobic and microaerophilic conditions. Am. Rev. Respir. Dis. 114:807-811.
    • (1976) Am. Rev. Respir. Dis. , vol.114 , pp. 807-811
    • Wayne, L.G.1
  • 38
    • 0019973896 scopus 로고
    • Glyoxylate metabolism and adaptation of Mycobacterium tuberculosis to survival under anaerobic conditions
    • Wayne, L. G., and K. Y. Lin. 1982. Glyoxylate metabolism and adaptation of Mycobacterium tuberculosis to survival under anaerobic conditions. Infect. Immun. 37:1042-1049.
    • (1982) Infect. Immun. , vol.37 , pp. 1042-1049
    • Wayne, L.G.1    Lin, K.Y.2
  • 39
    • 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
  • 40
    • 0022423148 scopus 로고
    • Domain structure and evolution in α-crystallins and small heat-shock proteins
    • Wistow, G. 1985. Domain structure and evolution in α-crystallins and small heat-shock proteins. FEBS Lett. 181:1-6.
    • (1985) FEBS Lett. , vol.181 , pp. 1-6
    • Wistow, G.1
  • 41
    • 0021760395 scopus 로고
    • The influence of messenger RNA secondary structure on expression of an immunoglobulin heavy chain in Escherichia coli
    • Wood, C. R., M. A. Boss, T. P. Patel, and J. S. Emtage. 1984. The influence of messenger RNA secondary structure on expression of an immunoglobulin heavy chain in Escherichia coli. Nucleic Acids Res. 12:3937-3950.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3937-3950
    • Wood, C.R.1    Boss, M.A.2    Patel, T.P.3    Emtage, J.S.4
  • 42
    • 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., and C. E. Barry III. 1996. Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of the mycobacterial α-crystallin homolog. J. Baeteriol. 178:4484-4492.
    • (1996) J. Baeteriol. , vol.178 , pp. 4484-4492
    • Yuan, Y.1    Crane, D.D.2    Barry C.E. III3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.