메뉴 건너뛰기




Volumn 26, Issue 4, 1997, Pages 821-831

Heat shock induction by a misassembled cytoplasmic membrane protein complex in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MALTODEXTRIN; MALTOSE; MEMBRANE PROTEIN;

EID: 0030695203     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.6271992.x     Document Type: Article
Times cited : (10)

References (44)
  • 2
    • 0030595346 scopus 로고    scopus 로고
    • Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies
    • Betton, J.M., Boscus, D., Missiakas, D., Raina, S., and Hofnung, M. (1996) Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J Mol Biol 262: 140-150.
    • (1996) J Mol Biol , vol.262 , pp. 140-150
    • Betton, J.M.1    Boscus, D.2    Missiakas, D.3    Raina, S.4    Hofnung, M.5
  • 3
    • 0024372724 scopus 로고
    • Positively charged amino acid residues can act as topogenic determinants in membrane proteins
    • Boyd, D., and Beckwith, J. (1989) Positively charged amino acid residues can act as topogenic determinants in membrane proteins. Proc Natl Acad Sci USA 86: 9446-9450.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9446-9450
    • Boyd, D.1    Beckwith, J.2
  • 4
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung, C.T., Niemela, S.L., and Miller, R.H. (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci USA 86: 2172-2175.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 5
    • 0025353955 scopus 로고
    • Cellular localization of the MalG protein from the maltose transport system in Escherichia coli
    • Dassa, E. (1990) Cellular localization of the MalG protein from the maltose transport system in Escherichia coli. Mol Gen Genet 222: 32-36.
    • (1990) Mol Gen Genet , vol.222 , pp. 32-36
    • Dassa, E.1
  • 6
    • 0027510078 scopus 로고
    • Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli
    • Dassa, E. (1993) Sequence-function relationships in MalG, an inner membrane protein from the maltose transport system in Escherichia coli. Mol Microbiol 7: 39-47.
    • (1993) Mol Microbiol , vol.7 , pp. 39-47
    • Dassa, E.1
  • 7
    • 0022125681 scopus 로고
    • Sequence of malG gene in E. coli K12: Homologies between integral membrane components from binding protein-dependent transport systems
    • Dassa, E., and Hofnung, M. (1985) Sequence of malG gene in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems. EMBO J 4: 2287-2293.
    • (1985) EMBO J , vol.4 , pp. 2287-2293
    • Dassa, E.1    Hofnung, M.2
  • 8
    • 0025214263 scopus 로고
    • Overproduction, solubilization and reconstitution of the maltose transport system from Escherichia coli
    • Davidson, A.L., and Nikaido, H. (1990) Overproduction, solubilization and reconstitution of the maltose transport system from Escherichia coli. J Biol Chem 265: 4254-4260.
    • (1990) J Biol Chem , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 9
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson, A.L., and Nikaido, H. (1991) Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli.. J Biol Chem 266: 8946-8951.
    • (1991) J Biol Chem , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 10
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans - Relevance to cystic fibrosis and multidrug resistance
    • Doige, C.A., and Ames, G.F.L (1993) ATP-dependent transport systems in bacteria and humans - relevance to cystic fibrosis and multidrug resistance. Annu Rev Microbiol 47: 291-319.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.L.2
  • 11
    • 0029975122 scopus 로고    scopus 로고
    • Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis
    • Ehrle, R., Pick, C., Ulrich, R., Hofmann, E., and Ehrmann, M. (1996) Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysis. J Bacteriol 178: 2255-2262.
    • (1996) J Bacteriol , vol.178 , pp. 2255-2262
    • Ehrle, R.1    Pick, C.2    Ulrich, R.3    Hofmann, E.4    Ehrmann, M.5
  • 12
    • 0024727149 scopus 로고
    • Identification of the sigma E subunit of Escherichia coli RNA polymerase: A second alternate sigma factor involved in high-temperature gene expression
    • Erickson, J.W., and Gross, C.A. (1989) Identification of the sigma E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression. Genes Dev 3: 1462-1471.
    • (1989) Genes Dev , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 13
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of E. coli
    • Froshauer, S., Green, G.N., Boyd, D., McGovern, K., and Beckwith, J. (1988) Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of E. coli. J Mol Biol 200: 501-511.
    • (1988) J Mol Biol , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 14
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heatshock promoters
    • Grossman, A.D., Erickson, J.W., and Gross, C.A. (1984) The htpR gene product of E. coli is a sigma factor for heatshock promoters. Cell 38: 383-390.
    • (1984) Cell , vol.38 , pp. 383-390
    • Grossman, A.D.1    Erickson, J.W.2    Gross, C.A.3
  • 15
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and Helenius, A. (1995) Quality control in the secretory pathway. Curr Opin Cell Biol 7: 523-9.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 16
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C.F. (1992) ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8: 67-113.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 17
    • 0030014628 scopus 로고    scopus 로고
    • Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion
    • Jander, G., Cronan, J.E., and Beckwith, J. (1996) Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion. J Bacteriol 178: 3049-3058.
    • (1996) J Bacteriol , vol.178 , pp. 3049-3058
    • Jander, G.1    Cronan, J.E.2    Beckwith, J.3
  • 18
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., and Riordan, J.R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-35.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 19
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R.D., and Sitia, R. (1990) Protein degradation in the endoplasmic reticulum. Cell 62: 611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 20
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82: 488-492.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 21
    • 0021719522 scopus 로고
    • Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor
    • Landick, R., Vaughn, V., Lau, E.T., VanBogelen, R.A., Erickson, J.W., and Neidhardt, F.C. (1984) Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor. Cell 38: 175-182.
    • (1984) Cell , vol.38 , pp. 175-182
    • Landick, R.1    Vaughn, V.2    Lau, E.T.3    Vanbogelen, R.A.4    Erickson, J.W.5    Neidhardt, F.C.6
  • 22
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S.W., and Kolter, R. (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-1773.
    • (1996) J Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 23
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the major outer membrane proteins of Escherichia coli into four bands
    • Lugtenberg, B., Meijers, J., Peters, R., van der Hoek, P., and van Alphen, L. (1975) Electrophoretic resolution of the major outer membrane proteins of Escherichia coli into four bands. FEBS Lett 58: 254-258.
    • (1975) FEBS Lett , vol.58 , pp. 254-258
    • Lugtenberg, B.1    Meijers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 24
    • 0025746244 scopus 로고
    • Membrane insertion of the Escherichia coli MalF protein in cells with impaired secretion machinery
    • McGovern, K., and Beckwith, J. (1991) Membrane insertion of the Escherichia coli MalF protein in cells with impaired secretion machinery. J Biol Chem 266: 20870-20876.
    • (1991) J Biol Chem , vol.266 , pp. 20870-20876
    • McGovern, K.1    Beckwith, J.2
  • 25
    • 0029610258 scopus 로고
    • Membrane protein assembly: Genetic, evolutionary and medical perspectives
    • Manoil, C., and Traxler, B. (1995) Membrane protein assembly: genetic, evolutionary and medical perspectives. Annu Rev Genet 29: 131-150.
    • (1995) Annu Rev Genet , vol.29 , pp. 131-150
    • Manoil, C.1    Traxler, B.2
  • 26
    • 0027787823 scopus 로고
    • The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas, J., Rouviere, P.E., Erickson, J.W., Donohue, T.J., and Gross, C.A. (1993) The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev 7: 2618-2628.
    • (1993) Genes Dev , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 27
  • 28
    • 0031081341 scopus 로고    scopus 로고
    • Protein misfolding in the cell envelope of Escherichia coli: New signaling pathways
    • Missiakas, D., and Raina, S. (1997) Protein misfolding in the cell envelope of Escherichia coli: new signaling pathways. Trends Biochem Sci 22: 59-63.
    • (1997) Trends Biochem Sci , vol.22 , pp. 59-63
    • Missiakas, D.1    Raina, S.2
  • 29
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., Betton, J.M., and Raina, S. (1996) New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 21: 871-884.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 30
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters - A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., Hofnung, M., and Dassa, E. (1997) Subunit interactions in ABC transporters - a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J 16: 3066-3077.
    • (1997) EMBO J , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 31
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido, H. (1994) Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett 346: 55-58.
    • (1994) FEBS Lett , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 32
    • 0027375813 scopus 로고
    • Characterization of the structural requirements for assembly and nucleotide binding of an ATP-Binding cassette transporter - The maltose transport system of Escherichia coli
    • Panagiotidis, C.H., Reyes, M., Sievertsen, A., Boos, W., and Shuman, H.A. (1993) Characterization of the structural requirements for assembly and nucleotide binding of an ATP-Binding cassette transporter - the maltose transport system of Escherichia coli. J Biol Chem 268: 23685-23696.
    • (1993) J Biol Chem , vol.268 , pp. 23685-23696
    • Panagiotidis, C.H.1    Reyes, M.2    Sievertsen, A.3    Boos, W.4    Shuman, H.A.5
  • 33
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
    • Parsell, D.A., and Sauer, R.T. (1989) Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev 3: 1226-1232.
    • (1989) Genes Dev , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 34
    • 0027264459 scopus 로고
    • Integral membrane protein structure - Transmembrane alpha-helices as autonomous folding domains
    • Popot, J.L. (1993) Integral membrane protein structure - transmembrane alpha-helices as autonomous folding domains. Curr Opin Struct Biol 3: 532-540.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 532-540
    • Popot, J.L.1
  • 35
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli
    • Raina, S., Missiakas, D., and Georgopoulos, C. (1995) The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli. EMBO J 14: 1043-55.
    • (1995) EMBO J , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 36
    • 0028907529 scopus 로고
    • rpoE, the gene encoding the second heat-shock sigma factor, sigma (E), in Escherichia coli
    • Rouviere, P.E., Penas, A.D.L., Mecsas, J., Lu, C.Z., Rudd, K.E., and Gross, C.A. (1995) rpoE, the gene encoding the second heat-shock sigma factor, sigma (E), in Escherichia coli. EMBO J 14: 1032-1042.
    • (1995) EMBO J , vol.14 , pp. 1032-1042
    • Rouviere, P.E.1    Penas, A.D.L.2    Mecsas, J.3    Lu, C.Z.4    Rudd, K.E.5    Gross, C.A.6
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal Biochem 166: 368-79.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 38
    • 0026469992 scopus 로고
    • Assembly of a heteroologomeric membrane protein complex
    • Traxler, B., and Beckwith, J. (1992) Assembly of a heteroologomeric membrane protein complex. Proc Natl Acad Sci USA 89: 10852-10856.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10852-10856
    • Traxler, B.1    Beckwith, J.2
  • 39
    • 15844393588 scopus 로고    scopus 로고
    • Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery
    • Traxler, B., and Murphy, C. (1996) Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery. J Biol Chem 271: 12394-12400.
    • (1996) J Biol Chem , vol.271 , pp. 12394-12400
    • Traxler, B.1    Murphy, C.2
  • 40
    • 0026688543 scopus 로고
    • The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli
    • Traxler, B., Lee, C., Boyd, D., and Beckwith, J. (1992) The dynamics of assembly of a cytoplasmic membrane protein in Escherichia coli. J Biol Chem 267: 5339-5345.
    • (1992) J Biol Chem , vol.267 , pp. 5339-5345
    • Traxler, B.1    Lee, C.2    Boyd, D.3    Beckwith, J.4
  • 41
    • 0026795955 scopus 로고
    • Large scale purification, nucleotide binding properties, and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex
    • Walter, C., Bentrup, K.H.Z., and Schneider, E. (1992) Large scale purification, nucleotide binding properties, and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex. J Biol Chem 267: 8863-8869.
    • (1992) J Biol Chem , vol.267 , pp. 8863-8869
    • Walter, C.1    Bentrup, K.H.Z.2    Schneider, E.3
  • 42
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S., and Kopito, R.R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83: 121-7.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 43
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild, J., Rossmeissl, P., Walter, W.A., and Gross, C.A. (1996) Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J Bacteriol 178: 3608-13.
    • (1996) J Bacteriol , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 44
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wülfing, C., and Plückthun, A. (1994) Protein folding in the periplasm of Escherichia coli. Mol Microbiol 12: 685-692.
    • (1994) Mol Microbiol , vol.12 , pp. 685-692
    • Wülfing, C.1    Plückthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.