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Volumn 39, Issue 3, 2001, Pages 162-167

Stress-shock Response of a Methylotrophic Bacterium Methylovorus sp. strain SS1 DSM 11726

Author keywords

Heat shock proteins; Methylovorus sp. Strain SS1; Stress response

Indexed keywords


EID: 0346657488     PISSN: 12258873     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (32)
  • 2
    • 0022863486 scopus 로고
    • Characterization of heat shock in Bacillus subtilis
    • Arnosti, D.N., V.L. Singer, and M.J. Chamberlin. 1986. Characterization of heat shock in Bacillus subtilis. J. Bacteriol. 168, 1243-1249.
    • (1986) J. Bacteriol. , vol.168 , pp. 1243-1249
    • Arnosti, D.N.1    Singer, V.L.2    Chamberlin, M.J.3
  • 4
    • 0346611515 scopus 로고    scopus 로고
    • Transcriptional induction of a carbon starvation gene during other starvation and stress challenges in Pseudomonas putida MK1: A role of a carbon starvation gene in general starvation and stress responses
    • Chitra, S., H.S. Lee, and Y. Kim. 1999. Transcriptional induction of a carbon starvation gene during other starvation and stress challenges in Pseudomonas putida MK1: A role of a carbon starvation gene in general starvation and stress responses. J. Microbiol 37, 141-147.
    • (1999) J. Microbiol , vol.37 , pp. 141-147
    • Chitra, S.1    Lee, H.S.2    Kim, Y.3
  • 5
  • 6
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer?
    • Craig, E.A. and C.A. Gross. 1991. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16, 135-140.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 135-140
    • Craig, E.A.1    Gross, C.A.2
  • 7
    • 0027954495 scopus 로고
    • Heat shock proteins as molecular chaperones
    • Craig, E.A. and J. Becker. 1994. Heat shock proteins as molecular chaperones. Enr. J. Biochem. 219, 11-23.
    • (1994) Enr. J. Biochem. , vol.219 , pp. 11-23
    • Craig, E.A.1    Becker, J.2
  • 8
    • 0024557026 scopus 로고
    • Physiological and genetic responses of bacteria to osmotic stress
    • Csonka, L.N. 1989. Physiological and genetic responses of bacteria to osmotic stress. Microbiol. Rev. 53, 121-147.
    • (1989) Microbiol. Rev. , vol.53 , pp. 121-147
    • Csonka, L.N.1
  • 9
    • 0025786078 scopus 로고
    • Oxidative stress response in Escherichia coli and Salmonella typhimurium
    • Fair, S.B. and T. Kogoma. 1991. Oxidative stress response in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55, 561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Fair, S.B.1    Kogoma, T.2
  • 10
    • 0346250732 scopus 로고    scopus 로고
    • Acid stress responses of Salmonella and E. coli: Survival mechanisms, regulation, and implications for pathogenesis
    • Foster, J.W. 2001. Acid stress responses of Salmonella and E. coli: Survival mechanisms, regulation, and implications for pathogenesis. J. Microbiol. 39, 89-94.
    • (2001) J. Microbiol. , vol.39 , pp. 89-94
    • Foster, J.W.1
  • 11
    • 0025872154 scopus 로고
    • A survey of the heat shock response in four Streptomyces species reveals two groEL-like genes and three GroEL-like proteins in Streptomyces albus
    • Guglielmi, G., P. Mazodier, C.J. Thompson, and J. Davies, 1991. A survey of the heat shock response in four Streptomyces species reveals two groEL-like genes and three GroEL-like proteins in Streptomyces albus. J. Bacteriol. 173, 7374-7381.
    • (1991) J. Bacteriol. , vol.173 , pp. 7374-7381
    • Guglielmi, G.1    Mazodier, P.2    Thompson, C.J.3    Davies, J.4
  • 12
    • 3042914268 scopus 로고    scopus 로고
    • Synthesis and requirement of Escherichia coli heat shock proteins GroEL and DnaK for survival under phenol stress conditions
    • Jeon, T.-J. and K.-J. Lee. 1998. Synthesis and requirement of Escherichia coli heat shock proteins GroEL and DnaK for survival under phenol stress conditions. J. Microbiol. 36, 26-33.
    • (1998) J. Microbiol. , vol.36 , pp. 26-33
    • Jeon, T.-J.1    Lee, K.-J.2
  • 13
    • 0019855290 scopus 로고
    • Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena
    • Kim, Y.M. and G.D. Hegeman. 1981. Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena. J. Bacteriol. 148, 904-911.
    • (1981) J. Bacteriol. , vol.148 , pp. 904-911
    • Kim, Y.M.1    Hegeman, G.D.2
  • 15
    • 0028290369 scopus 로고
    • Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance
    • Krüger, E., U.Völker, and M. Hecker. 1994. Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance. J. Bacteriol. 176, 3360-3367.
    • (1994) J. Bacteriol. , vol.176 , pp. 3360-3367
    • Krüger, E.1    Völker, U.2    Hecker, M.3
  • 16
    • 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
  • 17
    • 0023740042 scopus 로고
    • The relationship of heat shock proteins, thermotolerance and protein synthesis
    • Laszlo, A. 1988. The relationship of heat shock proteins, thermotolerance and protein synthesis. Exp. Cell Res. 179, 401-414.
    • (1988) Exp. Cell Res. , vol.179 , pp. 401-414
    • Laszlo, A.1
  • 18
    • 0022555843 scopus 로고
    • The heat shock response
    • Lindquist, S. 1986. The heat shock response. Annu. Rev. Biochem. 55, 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 19
    • 0023924166 scopus 로고
    • Characterization of the thermotolerant cell. I. Effect on protein synthesis activity and the regulation of heat shock protien 70 expression
    • Mizzen, L.A. and W.J. Welch. 1988. Characterization of the thermotolerant cell. I. Effect on protein synthesis activity and the regulation of heat shock protien 70 expression. J. Cell. Biol. 106, 1106-1116.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1106-1116
    • Mizzen, L.A.1    Welch, W.J.2
  • 21
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4121.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4121
    • O'Farrell, P.H.1
  • 22
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacry-lamide gels
    • Okaley, B.R., D.R. Kirsh, and N.R. Morris. 1980. A simplified ultrasensitive silver stain for detecting proteins in polyacry-lamide gels. Anal. Biochem. 105, 361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Okaley, B.R.1    Kirsh, D.R.2    Morris, N.R.3
  • 23
    • 0023660331 scopus 로고
    • Asymmetric segregation of heat shock proteins upon cell division in Caulobacter ere- Centus
    • Reuter, S.H. and L. Shapiro. 1987. Asymmetric segregation of heat shock proteins upon cell division in Caulobacter ere- centus. J. Mol. Biol. 194, 653-662.
    • (1987) J. Mol. Biol. , vol.194 , pp. 653-662
    • Reuter, S.H.1    Shapiro, L.2
  • 24
    • 0022518277 scopus 로고
    • Heat shock proteins in Bacillus subtilis: A two-dimensional gel electrophoresis study
    • Richter, A. and M. Hecker. 1986. Heat shock proteins in Bacillus subtilis: a two-dimensional gel electrophoresis study. FEMS Microbiol. Lett. 36, 69-71.
    • (1986) FEMS Microbiol. Lett. , vol.36 , pp. 69-71
    • Richter, A.1    Hecker, M.2
  • 25
    • 0027483509 scopus 로고
    • Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti
    • Rusanganwa, E. and R.S. Gupta. 1993. Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti. Gene 126, 67-75.
    • (1993) Gene , vol.126 , pp. 67-75
    • Rusanganwa, E.1    Gupta, R.S.2
  • 26
    • 0347532865 scopus 로고
    • Isolation and chatacterization of a restricted facultatively methylotrophic bacterium Methylovorus sp. strain SS1
    • Seo, S.A. and Y.M. Kim. 1993. Isolation and chatacterization of a restricted facultatively methylotrophic bacterium Methylovorus sp. strain SS1. Kor. J. Microbiol. 31, 179-183.
    • (1993) Kor. J. Microbiol. , vol.31 , pp. 179-183
    • Seo, S.A.1    Kim, Y.M.2
  • 27
    • 0027434222 scopus 로고
    • Use of new Escherichia coli/Streptomyces conjugative vectors to probe the functions of the two groEL-like genes of Streptomyces albuse G by gene disruption
    • Servant, P., C. Thompson, and P. Mazodier. 1993. Use of new Escherichia coli/Streptomyces conjugative vectors to probe the functions of the two groEL-like genes of Streptomyces albuse G by gene disruption. Gene 134, 25-32.
    • (1993) Gene , vol.134 , pp. 25-32
    • Servant, P.1    Thompson, C.2    Mazodier, P.3
  • 28
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • Trent, J.D., E. Nimmesgerm, J.S. Wall, F.U. HartI, and A.L. Horwich. 1991. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354, 490-493.
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgerm, E.2    Wall, J.S.3    Harti, F.U.4    Horwich, A.L.5
  • 29
    • 0024554109 scopus 로고
    • Escherichia coli proteins inducible by oxidation stress mediated by the Superoxide radical
    • Walkup, L, K.B. and T. Kogoma. 1989. Escherichia coli proteins inducible by oxidation stress mediated by the Superoxide radical. J. Bacteriol. 171, 1476-1484.
    • (1989) J. Bacteriol. , vol.171 , pp. 1476-1484
    • Walkup, L.1    B, K.2    Kogoma, T.3
  • 30
    • 38249033684 scopus 로고
    • The stress-shock response of the bacterium Methylophilus methylotrophus
    • Watt, P.W. and M.J. North. 1987. The stress-shock response of the bacterium Methylophilus methylotrophus. FEBS Lett. 215, 295-299.
    • (1987) FEBS Lett. , vol.215 , pp. 295-299
    • Watt, P.W.1    North, M.J.2
  • 31
    • 0014690791 scopus 로고
    • The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. and M. Osborn. 1969. The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 32
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., H. Nagai, and H. Mori. 1993. Regulation of the heat-shock response in bacteria. Microbiol. Rev. 47, 321-350.
    • (1993) Microbiol. Rev. , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3


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