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Volumn 25, Issue 5, 1997, Pages 933-944

Points mutations in the transmembrane domain of DjlA, a membrane-linked DnaJ-like protein, abolish its function in promoting colanic acid production via the Rcs signal transduction pathway

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; MEMBRANE PROTEIN; BACTERIAL DNA; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; BACTERIUM ANTIBODY; COLANIC ACID; DJLA PROTEIN, E COLI; DNAJ PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; MULTIENZYME COMPLEX; PHOSPHOPROTEIN PHOSPHATASE; POLYSACCHARIDE; PROTEIN KINASE; RCSB PROTEIN, BACTERIA; RCSB PROTEIN, E COLI; RCSC PROTEIN, BACTERIA; RCSC PROTEIN, E COLI; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR;

EID: 0030609138     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.1997.mmi528.x     Document Type: Article
Times cited : (51)

References (42)
  • 1
    • 0029779670 scopus 로고    scopus 로고
    • Mutational analysis of a transmembrane segment in a bacterial chemoreceptor
    • Baumgartner, J.W., and Hazelbauer, G.L. (1996) Mutational analysis of a transmembrane segment in a bacterial chemoreceptor. J Bacteriol 178: 4651-4660.
    • (1996) J Bacteriol , vol.178 , pp. 4651-4660
    • Baumgartner, J.W.1    Hazelbauer, G.L.2
  • 2
    • 0023933251 scopus 로고
    • Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12
    • Brill, J.A., Quinlan-Walshe, C., and Gottesman, S. (1988) Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12. J Bacteriol 170: 2599-2611.
    • (1988) J Bacteriol , vol.170 , pp. 2599-2611
    • Brill, J.A.1    Quinlan-Walshe, C.2    Gottesman, S.3
  • 3
    • 0028898217 scopus 로고
    • Hormone-dependent transactivation by the human androgen receptor is regulated by a DnaJ protein
    • Caplan, A.J., Langley, E., Wilson, E., and Vidal, J. (1995) Hormone-dependent transactivation by the human androgen receptor is regulated by a DnaJ protein. J Biol Chem 270: 5251-5257.
    • (1995) J Biol Chem , vol.270 , pp. 5251-5257
    • Caplan, A.J.1    Langley, E.2    Wilson, E.3    Vidal, J.4
  • 4
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casabadan, M.J. (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104: 541-555.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casabadan, M.J.1
  • 6
    • 0029900569 scopus 로고    scopus 로고
    • A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a Type III topology
    • Clarke, D.J., Jacq, A., and Holland, I.B. (1996) A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a Type III topology. Mol Microbiol 20: 1273-1286.
    • (1996) Mol Microbiol , vol.20 , pp. 1273-1286
    • Clarke, D.J.1    Jacq, A.2    Holland, I.B.3
  • 7
    • 9044242892 scopus 로고
    • Regulation of exopolysaccharide synthesis in Erwinia stewartii by rcsB and rcsC
    • Coplin, D.L., Poetter, K., and Majerczak, D.R. (1990) Regulation of exopolysaccharide synthesis in Erwinia stewartii by rcsB and rcsC. Phytopathology 81: 1220.
    • (1990) Phytopathology , vol.81 , pp. 1220
    • Coplin, D.L.1    Poetter, K.2    Majerczak, D.R.3
  • 8
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of Class II MHC molecules
    • Cosson, P., and Bonifacino, J.S. (1992) Role of transmembrane domain interactions in the assembly of Class II MHC molecules. Science 258: 659-662.
    • (1992) Science , vol.258 , pp. 659-662
    • Cosson, P.1    Bonifacino, J.S.2
  • 9
    • 0025819126 scopus 로고
    • Membrane protein association by potential intramembrane charge pairs
    • Cosson, P., Lankford, S.P., Bonafacino, J.S., and Klausner, R.D. (1991) Membrane protein association by potential intramembrane charge pairs. Nature 351: 414-416.
    • (1991) Nature , vol.351 , pp. 414-416
    • Cosson, P.1    Lankford, S.P.2    Bonafacino, J.S.3    Klausner, R.D.4
  • 11
    • 0026740416 scopus 로고
    • The rcsB gene, a positive regulator of colanic acid biosynthesis in Escherichia coli, is also activator of ftsZ expression
    • Gervais, F.G., Phoneix, P., and Drapeau, G.R. (1992) The rcsB gene, a positive regulator of colanic acid biosynthesis in Escherichia coli, is also activator of ftsZ expression. J Bacteriol 174: 3964-3971.
    • (1992) J Bacteriol , vol.174 , pp. 3964-3971
    • Gervais, F.G.1    Phoneix, P.2    Drapeau, G.R.3
  • 12
    • 0000871346 scopus 로고
    • Regulation of capsule synthesis: Modification of the two-component paradigm by an accessory unstable regulator
    • Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society of Microbiology
    • Gottesman, S. (1995) Regulation of capsule synthesis: modification of the two-component paradigm by an accessory unstable regulator. In Two-component signal transduction. Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society of Microbiology, pp, 253-262.
    • (1995) Two-component Signal Transduction , pp. 253-262
    • Gottesman, S.1
  • 14
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F-U. (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 15
    • 0022462026 scopus 로고
    • A complete library of point mutations in the glucocorticoid response element of mouse mammary tumor virus
    • Hutchinson, III, C.A., Nordeen, S.K., Vogt, K., and Edgell, M.H. (1986) A complete library of point mutations in the glucocorticoid response element of mouse mammary tumor virus. Proc Natl Acad Sci USA 83: 710-714.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 710-714
    • Hutchinson III, C.A.1    Nordeen, S.K.2    Vogt, K.3    Edgell, M.H.4
  • 16
    • 0030883403 scopus 로고    scopus 로고
    • Positive control of the two-component RcsC/B signal transduction network by DjIA: A member of the DnaJ family of molecular chaperones in Escherichia coli
    • Kelley, W., and Georgopoulos, C. (1997) Positive control of the two-component RcsC/B signal transduction network by DjIA: a member of the DnaJ family of molecular chaperones in Escherichia coli. Mol Microbiol 25: 913-921.
    • (1997) Mol Microbiol , vol.25 , pp. 913-921
    • Kelley, W.1    Georgopoulos, C.2
  • 17
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the Glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch, D., Brosig, B., Kolmar, H., and Fritz, H.-J. (1996) Dimerisation of the Glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J Mol Biol 263: 525-530.
    • (1996) J Mol Biol , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.-J.4
  • 19
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M., and Engelman, D.M. (1994) Specificity and promiscuity in membrane helix interactions. Q Rev Biophysics 27: 157-218.
    • (1994) Q Rev Biophysics , vol.27 , pp. 157-218
    • Lemmon, M.1    Engelman, D.M.2
  • 21
  • 22
    • 0029052538 scopus 로고
    • The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the σ32 heat shock transcriptional regulator
    • Liberek, K., Wall, D., and Georgopoulos, C. (1995) The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the σ32 heat shock transcriptional regulator. Proc Natl Acad Sci USA 92: 6224-6228.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6224-6228
    • Liberek, K.1    Wall, D.2    Georgopoulos, C.3
  • 23
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K.R., Prestegard, J.H., and Engelman, D.M. (1997) A transmembrane helix dimer: structure and implications. Science 276: 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 24
    • 0031013877 scopus 로고    scopus 로고
    • The molecular chaperone Hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR
    • Melville, M.W., Hansen, W.J., Freeman, B.C., Welch, W.J., and Katze, M.G. (1997) The molecular chaperone Hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR. Proc Natl Acad Sci USA 94: 97-102.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 97-102
    • Melville, M.W.1    Hansen, W.J.2    Freeman, B.C.3    Welch, W.J.4    Katze, M.G.5
  • 26
    • 0017624645 scopus 로고
    • Selection of Ion mutants in E. coli by treatment with phenothiazines
    • Molnar, J., Holland, I.B., and Mandi, Y. (1977) Selection of Ion mutants in E. coli by treatment with phenothiazines. Genet Res 30: 13-20.
    • (1977) Genet Res , vol.30 , pp. 13-20
    • Molnar, J.1    Holland, I.B.2    Mandi, Y.3
  • 27
    • 0028097873 scopus 로고
    • A role for exoplysaccharides in the protection of microorganisms from dessication
    • Ophir, T., and Gutnick, D.L. (1994) A role for exoplysaccharides in the protection of microorganisms from dessication. Appl Environ Microbiol 60: 740-745.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 740-745
    • Ophir, T.1    Gutnick, D.L.2
  • 28
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C., and Wüthrich, K. (1996) NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 260: 236-250.
    • (1996) J Mol Biol , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 29
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear Magnetic Resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y.Q., Patel, D., Hartl, F.-U., and McColl, D.J. (1996) Nuclear Magnetic Resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol 260: 224-235.
    • (1996) J Mol Biol , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.-U.3    McColl, D.J.4
  • 30
    • 0025164669 scopus 로고
    • Isolation and characterization of dnaJ null mutants of Escherichia coli
    • Sell, S.M., Eisen, C., Ang, D., Zyclicz, M., and Georgopoulos, C. (1990) Isolation and characterization of dnaJ null mutants of Escherichia coli. J Bacteriol 172: 4827-4835.
    • (1990) J Bacteriol , vol.172 , pp. 4827-4835
    • Sell, S.M.1    Eisen, C.2    Ang, D.3    Zyclicz, M.4    Georgopoulos, C.5
  • 31
    • 0030029879 scopus 로고    scopus 로고
    • Osmotic shock induction of capsule synthesis in Escherichia coli K-12
    • Sledjeski, D.D., and Gottesman, S. (1996) Osmotic shock induction of capsule synthesis in Escherichia coli K-12. J Bacteriol 178: 1204-1206.
    • (1996) J Bacteriol , vol.178 , pp. 1204-1206
    • Sledjeski, D.D.1    Gottesman, S.2
  • 32
    • 0028814024 scopus 로고
    • Determination of helix-helix interactions in membranes by rotational resonance NMR
    • Smith, S.O., and Bormann, B. (1995) Determination of helix-helix interactions in membranes by rotational resonance NMR. Proc Natl Acad Sci USA 92: 488-491.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 488-491
    • Smith, S.O.1    Bormann, B.2
  • 33
    • 0029779295 scopus 로고    scopus 로고
    • Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid
    • Stevenson, G., Andrianopoulos, K., Hobbs, M., and Reeves, P.R. (1996) Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid. J Bacteriol 178: 4885-4893.
    • (1996) J Bacteriol , vol.178 , pp. 4885-4893
    • Stevenson, G.1    Andrianopoulos, K.2    Hobbs, M.3    Reeves, P.R.4
  • 34
    • 0025095229 scopus 로고
    • RcsB and RcsC: A two-component regulator of capsular synthesis in Escherichia coli
    • Stout, V., and Gottesman, S. (1990) RcsB and RcsC: a two-component regulator of capsular synthesis in Escherichia coli. J Bacteriol 172: 659-669.
    • (1990) J Bacteriol , vol.172 , pp. 659-669
    • Stout, V.1    Gottesman, S.2
  • 35
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo, A., Korszun, R., Hartl, F.-U., and Flanagan, J. (1996) A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 15: 408-417.
    • (1996) EMBO J , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.-U.3    Flanagan, J.4
  • 36
    • 0023131531 scopus 로고
    • Capsule synthesis in Escherichia coli is regulated by proteolysis
    • Torres-Cabassa, A.S., and Gottesman, S. (1987) Capsule synthesis in Escherichia coli is regulated by proteolysis. J Bacteriol 169: 981-989.
    • (1987) J Bacteriol , vol.169 , pp. 981-989
    • Torres-Cabassa, A.S.1    Gottesman, S.2
  • 37
    • 0027979545 scopus 로고
    • An analogue of the DnaJ molecular chaperone in Escherichia coli
    • Ueguchi, C., Kakeda, M., Yamada, H., and Mizuno, T. (1994) An analogue of the DnaJ molecular chaperone in Escherichia coli. Proc Natl Acad Sci USA 91: 1054-1058.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1054-1058
    • Ueguchi, C.1    Kakeda, M.2    Yamada, H.3    Mizuno, T.4
  • 38
    • 0029034167 scopus 로고
    • A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
    • Ueguchi, C., Shiozawa, T., Kakeda, M., Yamada, H., and Mizuno, T. (1995) A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J Bacteriol 177: 3894-3896.
    • (1995) J Bacteriol , vol.177 , pp. 3894-3896
    • Ueguchi, C.1    Shiozawa, T.2    Kakeda, M.3    Yamada, H.4    Mizuno, T.5
  • 39
    • 0029928659 scopus 로고    scopus 로고
    • Characterization of the rcsA and rcsB genes from Salmonella typhi: RcsB through tviA is involved in regulation of Vi antigen synthesis
    • Virlogeux, I., Waxin, H., Ecobichon, C., Lee, J.O., and Popoff, M.Y. (1996) Characterization of the rcsA and rcsB genes from Salmonella typhi: rcsB through tviA is involved in regulation of Vi antigen synthesis. J Bacteriol 178: 1691-1698.
    • (1996) J Bacteriol , vol.178 , pp. 1691-1698
    • Virlogeux, I.1    Waxin, H.2    Ecobichon, C.3    Lee, J.O.4    Popoff, M.Y.5
  • 40
    • 0028170215 scopus 로고
    • The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
    • Wall, D., Zylicz, M., and Georgopoulos, C. (1994) The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J Biol Chem 269: 5446-5451.
    • (1994) J Biol Chem , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 42
    • 0028991053 scopus 로고
    • Analysis of a Coxiella burnetti gene product that activates capsule synthesis in Escherichia coli: Requirement for the heat shock chaperone DnaK and the two-component regulator RcsC
    • Zuber, M., Hoover, T.A., and Court, D.L. (1995) Analysis of a Coxiella burnetti gene product that activates capsule synthesis in Escherichia coli: requirement for the heat shock chaperone DnaK and the two-component regulator RcsC. J Bacteriol 177: 4238-4244.
    • (1995) J Bacteriol , vol.177 , pp. 4238-4244
    • Zuber, M.1    Hoover, T.A.2    Court, D.L.3


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