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Volumn 186, Issue 23, 2004, Pages 8149-8152

The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CITRATE SYNTHASE; GLUTAMATE 5 KINASE; PROLINE; PROTEIN DNAK; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 9244263009     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.23.8149-8152.2004     Document Type: Article
Times cited : (76)

References (22)
  • 1
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T., and S. N. Timasheff. 1985. The stabilization of proteins by osmolytes. Biophys. J. 47:411-414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 2
    • 0014696505 scopus 로고
    • Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase
    • Baich, A. 1969. Proline synthesis in Escherichia coli. A proline-inhibitable glutamic acid kinase. Biochim. Biophys. Acta 192:462-467.
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 462-467
    • Baich, A.1
  • 5
    • 0019348460 scopus 로고
    • Proline over-production results in enhanced osmotolerance in Salmonella typhimurium
    • Csonka, L. N. 1981. Proline over-production results in enhanced osmotolerance in Salmonella typhimurium. Mol. Gen. Genet. 182:82-86.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 82-86
    • Csonka, L.N.1
  • 6
    • 0020369542 scopus 로고
    • A third L-proline permease in Salmonella typhimurium which functions in media of elevated osmotic strength
    • Csonka, L. N. 1982. A third L-proline permease in Salmonella typhimurium which functions in media of elevated osmotic strength. J. Bacteriol. 151:1433-1443.
    • (1982) J. Bacteriol. , vol.151 , pp. 1433-1443
    • Csonka, L.N.1
  • 7
    • 0023905532 scopus 로고
    • Regulation of cytoplasmic praline levels in Salmonella typhimurium: Effect of osmotic stress on synthesis, degradation, and cellular retention of proline
    • Csonka, L. N. 1988. Regulation of cytoplasmic praline levels in Salmonella typhimurium: effect of osmotic stress on synthesis, degradation, and cellular retention of proline. J. Bacteriol. 170:2374-2378.
    • (1988) J. Bacteriol. , vol.170 , pp. 2374-2378
    • Csonka, L.N.1
  • 8
    • 0024219907 scopus 로고
    • A single base pair change in proline biosynthesis genes causes osmotic stress tolerance
    • Dandekar, A. M., and S. L. Uratsu. 1988. A single base pair change in proline biosynthesis genes causes osmotic stress tolerance. J. Bacteriol. 170:5943-5945.
    • (1988) J. Bacteriol. , vol.170 , pp. 5943-5945
    • Dandekar, A.M.1    Uratsu, S.L.2
  • 9
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant, S., N. Eliahu, D. Rosenthal, and P. Goloubinoff. 2001. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276:39586-39591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 10
    • 0037344041 scopus 로고    scopus 로고
    • Proteomic analysis of Lactococcus lactis, a lactic acid bacterium
    • Guillot, A., C. Gitton, P. Anglade, and M. Y. Mistou. 2003. Proteomic analysis of Lactococcus lactis, a lactic acid bacterium. Proteomics 3:337-354.
    • (2003) Proteomics , vol.3 , pp. 337-354
    • Guillot, A.1    Gitton, C.2    Anglade, P.3    Mistou, M.Y.4
  • 11
    • 0036887272 scopus 로고    scopus 로고
    • In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures
    • Gur, E., D. Biran, E. Gazit, and E. Z. Ron. 2002. In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures. Mol. Microbiol. 46:1391-1397.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1391-1397
    • Gur, E.1    Biran, D.2    Gazit, E.3    Ron, E.Z.4
  • 12
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U., and M. Hayer-Hartl. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 13
    • 0026330981 scopus 로고
    • Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli
    • Hengge-Aronis, R., W. Klein, R. Lange, M. Rimmele, and W. Boos. 1991. Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli. J. Bacteriol. 173:7918-7924.
    • (1991) J. Bacteriol. , vol.173 , pp. 7918-7924
    • Hengge-Aronis, R.1    Klein, W.2    Lange, R.3    Rimmele, M.4    Boos, W.5
  • 14
    • 0031719418 scopus 로고    scopus 로고
    • Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments
    • Kempf, B., and E. Bremer. 1998. Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments. Arch. Microbiol. 170:310-330.
    • (1998) Arch. Microbiol. , vol.170 , pp. 310-330
    • Kempf, B.1    Bremer, E.2
  • 15
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., T. Tomoyasu, P. Goloubinoff, S. Rüdiger, D. Röder, H. Langen, and B. Bukau. 1999. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18:6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Röder, D.5    Langen, H.6    Bukau, B.7
  • 16
    • 0023123175 scopus 로고
    • Escherichia coli dnaK null mutants are inviable at high temperature
    • Paek, K. H., and G. C. Walker. 1987. Escherichia coli dnaK null mutants are inviable at high temperature. J. Bacteriol. 169:283-290.
    • (1987) J. Bacteriol. , vol.169 , pp. 283-290
    • Paek, K.H.1    Walker, G.C.2
  • 17
    • 0021939776 scopus 로고
    • Glycine betaine transport in Escherichia coli: Osmotic modulation
    • Perroud, B., and D. Le Rudulier. 1985. Glycine betaine transport in Escherichia coli: osmotic modulation. J. Bacteriol. 161:393-401.
    • (1985) J. Bacteriol. , vol.161 , pp. 393-401
    • Perroud, B.1    Le Rudulier, D.2
  • 18
    • 0031004715 scopus 로고    scopus 로고
    • Chaperone properties of the bacterial periplasmic substrate-binding proteins
    • Richarme, G., and T. D. Caldas. 1997. Chaperone properties of the bacterial periplasmic substrate-binding proteins. J. Biol. Chem. 272:15607-15612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15607-15612
    • Richarme, G.1    Caldas, T.D.2
  • 19
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt, J., S. B. Prusiner, and W. J. Welch. 1996. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15:6363-6373.
    • (1996) EMBO J. , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 20
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of proteins in dilute solution in the presence of detergents and lipids
    • Wessel, D., and U. I. Flugge. 1984. A method for the quantitative recovery of proteins in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 21
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P. H., M. E. Clark, S. C. Hand, R. D. Bowlus, and G. N. Somero. 1982. Living with water stress: evolution of osmolyte systems. Science 217:1214-1222.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 22
    • 0037881834 scopus 로고    scopus 로고
    • Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli
    • Zhu, W., and D. F. Becker. 2003. Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli. Biochemistry 42:5469-5477.
    • (2003) Biochemistry , vol.42 , pp. 5469-5477
    • Zhu, W.1    Becker, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.