메뉴 건너뛰기




Volumn 194, Issue 1, 1997, Pages 1-8

Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37°C but not at 43°C

Author keywords

Heat shock; Molecular chaperones; Protein folding

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN;

EID: 0030846353     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00087-5     Document Type: Article
Times cited : (34)

References (24)
  • 1
    • 0022613101 scopus 로고
    • Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes
    • Fayet, O., Louarn, J-M., Georgopoulos, C., 1986. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. J. Bacteriol. 202, 435-445.
    • (1986) J. Bacteriol. , vol.202 , pp. 435-445
    • Fayet, O.1    Louarn, J.-M.2    Georgopoulos, C.3
  • 2
    • 0024554107 scopus 로고
    • The groES and groEL heat shock products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet, O., Ziegelhoffer, T., Georgopoulos, C., 1989. The groES and groEL heat shock products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 3
    • 0020793569 scopus 로고
    • A technique for radiolabelling DNA restriction endonuclease fragments to a high specific activity
    • Feinberg, A.P., Vogelstein, B., 1983. A technique for radiolabelling DNA restriction endonuclease fragments to a high specific activity. Anal. Biochem. 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 4
    • 0029121223 scopus 로고
    • Identification of GroEL as a constituent of an mRNA protection complex in Escherichia coli
    • Georgellis, D., Sohlberg, B., Harlt, F.-U., von Gabain, A., 1995. Identification of GroEL as a constituent of an mRNA protection complex in Escherichia coli. Mol. Microbiol. 16, 1259-1268.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1259-1268
    • Georgellis, D.1    Sohlberg, B.2    Harlt, F.-U.3    Von Gabain, A.4
  • 5
    • 0024578552 scopus 로고
    • GroE heat-shock proteins promote association of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff, P., Gatenby, A.A., Lorimer, G.H., 1989. GroE heat-shock proteins promote association of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337, 44-47.
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 7
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high level expression by vectors containing the pBAD promoter
    • Guzman, L.-M., Belin, D., Carson, M.J., Beckwith, J., 1995. Tight regulation, modulation, and high level expression by vectors containing the pBAD promoter. J. Bacteriol. 177, 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 8
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E., Lane, D., 1988. Antibodies. A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies. A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 9
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl, F.-U., Hlodan, R., Langer, T., 1994. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19, 20-25.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 10
    • 0027184721 scopus 로고
    • Molecular chaperones functions of heat shock proteins
    • Hendrick, J.P. and Hartl, F.-U., 1993. Molecular chaperones functions of heat shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 11
    • 0018776963 scopus 로고
    • Levels of major proteins of Escherichia coli during growth at different temperatures
    • Herendeen, S.L., van Bogelen, R.A., Neidhardt, F.C., 1979. Levels of major proteins of Escherichia coli during growth at different temperatures. J. Bacteriol. 139, 345-351.
    • (1979) J. Bacteriol. , vol.139 , pp. 345-351
    • Herendeen, S.L.1    Van Bogelen, R.A.2    Neidhardt, F.C.3
  • 12
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A.L., Low, K.B., Fenton, W.A., Hirshfield, I.N., Furtak, K., 1993. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74, 909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 13
    • 0028341060 scopus 로고
    • Effects of reduced levels of GroE chaperones on protein metabolism: Enhanced synthesis of heat shock proteins during steady state growth of Escherichia coli
    • Kanemori, M., Mori, H., Yura, T., 1994. Effects of reduced levels of GroE chaperones on protein metabolism: enhanced synthesis of heat shock proteins during steady state growth of Escherichia coli. J. Bacteriol. 176, 4235-4242.
    • (1994) J. Bacteriol. , vol.176 , pp. 4235-4242
    • Kanemori, M.1    Mori, H.2    Yura, T.3
  • 14
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., Zakour, R.A., 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Meth. Enzymol. 154, 367-382.
    • (1987) Meth. Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 15
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of chaperonin proteins in protein-folding in vivo
    • Lorimer, G.H., 1996. A quantitative assessment of the role of chaperonin proteins in protein-folding in vivo. FASEB J. 10, 5-9.
    • (1996) FASEB J. , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 17
    • 0017861127 scopus 로고
    • Patterns of protein synthesis in E. Coli. A catalogue of amount of 140 individual proteins at different growth rates
    • Pedersen, S., Bloch, P.L., Reeh, S., Neidhardt, F.C., 1978. Patterns of protein synthesis in E. coli. A catalogue of amount of 140 individual proteins at different growth rates. Cell 14, 179-190.
    • (1978) Cell , vol.14 , pp. 179-190
    • Pedersen, S.1    Bloch, P.L.2    Reeh, S.3    Neidhardt, F.C.4
  • 18
    • 0025375220 scopus 로고
    • Heat shock proteins DnaK and GroEL facilitate export of lacZ hybrid proteins in Escherichia coli
    • Phillips, G.J., Silhavy, T.J., 1990. Heat shock proteins DnaK and GroEL facilitate export of lacZ hybrid proteins in Escherichia coli. Nature 344, 882-884.
    • (1990) Nature , vol.344 , pp. 882-884
    • Phillips, G.J.1    Silhavy, T.J.2
  • 19
    • 0024582080 scopus 로고
    • Chromosomal transformation of Escherichia coli recD strains with linearized plasmids
    • Russell, C.B., Thaler D.S., Dahlquist, F.W., 1989. Chromosomal transformation of Escherichia coli recD strains with linearized plasmids. J. Bacteriol. 171, 2609-2613.
    • (1989) J. Bacteriol. , vol.171 , pp. 2609-2613
    • Russell, C.B.1    Thaler, D.S.2    Dahlquist, F.W.3
  • 21
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J., Messing, J., 1987. Production of single-stranded plasmid DNA. Meth. Enzymol. 153, 3-11
    • (1987) Meth. Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 22
    • 0027065105 scopus 로고
    • Purified chaperonin 60 GroEL] interacts with the non-native states of a multitude of Escherichia coli proteins
    • Viitanen, P.V., Gatenby, A.A., Lorimer, G.H., 1992. Purified chaperonin 60 (GroEL] interacts with the non-native states of a multitude of Escherichia coli proteins. Protein Sci. 1, 363-369.
    • (1992) Protein Sci. , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 23
    • 0028091148 scopus 로고
    • Rhizobium leguminosarum possesses multiple chaperonin 60 (cpn60) genes
    • Wallington, E.J. and Lund, P.A., 1994. Rhizobium leguminosarum possesses multiple chaperonin 60 (cpn60) genes. Microbiology 140, 113-122
    • (1994) Microbiology , vol.140 , pp. 113-122
    • Wallington, E.J.1    Lund, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.