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Volumn 251, Issue 1, 2005, Pages 75-80

Osmoregulation of the HtrA (DegP) protease of Escherichia coli: An Hha-H-NS complex represses HtrA expression at low osmolarity

Author keywords

Escherichia coli; H NS; Hha; HtrA; Osmoregulation

Indexed keywords

HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; PROTEIN HTRA; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 24944509074     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.07.027     Document Type: Article
Times cited : (14)

References (45)
  • 1
    • 0024519269 scopus 로고
    • Identification, characterization and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • B. Lipinska, O. Fayet, L. Baird, and C. Georgopoulos Identification, characterization and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures J. Bacteriol. 171 1989 1574 1584
    • (1989) J. Bacteriol. , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 2
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • K.L. Strauch, K. Johnson, and J. Beckwith Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature J. Bacteriol. 171 1989 2689 2696
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 3
    • 0030566837 scopus 로고    scopus 로고
    • Primary structure of a putative serine protease specific for IGF binding proteins
    • J. Zumbrun, and B. Trueb Primary structure of a putative serine protease specific for IGF binding proteins FEBS Lett. 398 1996 187 192
    • (1996) FEBS Lett. , vol.398 , pp. 187-192
    • Zumbrun, J.1    Trueb, B.2
  • 4
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • C.P. Ponting Evidence for PDZ domains in bacteria, yeast, and plants Protein Sci. 6 1997 464 468
    • (1997) Protein Sci. , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 5
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • M.J. Pallen, and B.W. Wren The HtrA family of serine proteases Mol. Microbiol. 26 1997 209 221
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 6
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • T. Clausen, C. Southan, and M. Ehrman The HtrA family of proteases: implications for protein composition and cell fate Mol. Cell. 10 2002 443 455
    • (2002) Mol. Cell. , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrman, M.3
  • 8
    • 0033617146 scopus 로고    scopus 로고
    • A temperature dependent switch from chaperone to protease in a widely conserved shock protein
    • C. Spiess, A. Beil, and M. Ehrmann A temperature dependent switch from chaperone to protease in a widely conserved shock protein Cell 97 1999 339 347
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 9
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperon machine
    • T. Krojer, M. Garrido-Franco, M. Huber, M. Ehrmann, and T. Clausen Crystal structure of DegP (HtrA) reveals a new protease-chaperon machine Nature 416 2002 455 459
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, M.3    Ehrmann, M.4    Clausen, T.5
  • 10
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • P.R. Waller, and R.T. Sauer Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease J. Bacteriol. 178 1996 1146 1153
    • (1996) J. Bacteriol. , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 11
    • 0030034915 scopus 로고    scopus 로고
    • Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA
    • J.C. Boucher, J. Martinez-Salazar, M.J. Schurr, M. Mudd, H. Yu, and V. Deretic Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA J. Bacteriol. 178 1996 511 523
    • (1996) J. Bacteriol. , vol.178 , pp. 511-523
    • Boucher, J.C.1    Martinez-Salazar, J.2    Schurr, M.J.3    Mudd, M.4    Yu, H.5    Deretic, V.6
  • 12
  • 14
    • 2542617706 scopus 로고    scopus 로고
    • Role of the HtrA in the virulence and competence of Streptococcus pneumoniae
    • Y.M. Ibrahim, A.R. Kerr, J. McCluskey, and T.J. Mitchell Role of the HtrA in the virulence and competence of Streptococcus pneumoniae Infect. Immun. 72 2004 3584 3591
    • (2004) Infect. Immun. , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1    Kerr, A.R.2    McCluskey, J.3    Mitchell, T.J.4
  • 15
    • 0034868619 scopus 로고    scopus 로고
    • Conserved DegP protease in Gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
    • C.H. Jones, T.C. Bolken, K.F. Jones, G.O. Zeller, and D.E. Hruby Conserved DegP protease in Gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes Infect. Immun. 69 2001 5538 5545
    • (2001) Infect. Immun. , vol.69 , pp. 5538-5545
    • Jones, C.H.1    Bolken, T.C.2    Jones, K.F.3    Zeller, G.O.4    Hruby, D.E.5
  • 16
    • 0025317783 scopus 로고
    • The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
    • B. Lipinska, M. Zylicz, and C. Georgopoulos The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase J. Bacteriol. 172 1990 1791 1797
    • (1990) J. Bacteriol. , vol.172 , pp. 1791-1797
    • Lipinska, B.1    Zylicz, M.2    Georgopoulos, C.3
  • 18
    • 0027787823 scopus 로고
    • e, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins Genes Dev. 7 1993 2618 2628
    • (1993) Genes Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouvière, P.E.2    Eriksson, J.W.3    Donohue, T.J.4    Gross, C.5
  • 19
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • D. Missiakas, J.M. Betton, and S. Raina New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH Mol. Microbiol. 21 1996 871 884
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 20
    • 0033106492 scopus 로고    scopus 로고
    • The σe and Cpx regulatory pathways: Overlapping but distinct envelope stress responses
    • T.L. Raivio, and T.J. Silhavy The σE and Cpx regulatory pathways: overlapping but distinct envelope stress responses Curr. Opin. Microbiol. 2 1999 159 165
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 21
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates the stress-inducible periplasmic protease, DegP
    • P.N. Danese, W.B. Snyder, C.L. Cosma, L.J.B. Davis, and T.J. Silhavy The Cpx two-component signal transduction pathway of Escherichia coli regulates the stress-inducible periplasmic protease, DegP Genes Dev. 9 1995 387 398
    • (1995) Genes Dev. , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.B.4    Silhavy, T.J.5
  • 22
    • 0031081341 scopus 로고    scopus 로고
    • Protein misfolding in the cell envelope of Escherichia coli: New signaling pathways
    • D. Missiakas, and S. Raina Protein misfolding in the cell envelope of Escherichia coli: new signaling pathways Trends Biochem. Sci. 22 1997 59 63
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 59-63
    • Missiakas, D.1    Raina, S.2
  • 23
    • 0033559269 scopus 로고    scopus 로고
    • Massive presence of the Escherichia coli "major cold-shock protein" CspA under non-stress conditions
    • A. Brandi, R. Spurio, C.O. Gualerzi, and C.L. Pon Massive presence of the Escherichia coli "major cold-shock protein" CspA under non-stress conditions EMBO J. 18 1999 1653 1659
    • (1999) EMBO J. , vol.18 , pp. 1653-1659
    • Brandi, A.1    Spurio, R.2    Gualerzi, C.O.3    Pon, C.L.4
  • 24
    • 0028036767 scopus 로고
    • The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to cold environment
    • P. Dersch, S. Kneip, and E. Bremer The nucleoid-associated DNA-binding protein H-NS is required for the efficient adaptation of Escherichia coli K-12 to cold environment Mol. Gen. Genet. 245 1994 255 259
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 255-259
    • Dersch, P.1    Kneip, S.2    Bremer, E.3
  • 25
    • 0031663584 scopus 로고    scopus 로고
    • Temperature sensing in bacterial gene regulation - What it all boils down to
    • R. Hurme, and M. Rhen Temperature sensing in bacterial gene regulation - what it all boils down to Mol. Microbiol. 30 1998 1 6
    • (1998) Mol. Microbiol. , vol.30 , pp. 1-6
    • Hurme, R.1    Rhen, M.2
  • 26
    • 0027450801 scopus 로고
    • Gene 5.5 protein of bacteriophage T7 inhibits the nucleoid protein H-NS of Escherichia coli
    • Q. Liu, and C. Richardson Gene 5.5 protein of bacteriophage T7 inhibits the nucleoid protein H-NS of Escherichia coli Proc. Natl. Acad. Sci. USA 90 1993 1761 1765
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1761-1765
    • Liu, Q.1    Richardson, C.2
  • 27
    • 0029932448 scopus 로고    scopus 로고
    • Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast
    • D.L. Marykwas, S.A. Schmidt, and H.C. Berg Interacting components of the flagellar motor of Escherichia coli revealed by the two-hybrid system in yeast J. Mol. Biol. 256 1996 564 576
    • (1996) J. Mol. Biol. , vol.256 , pp. 564-576
    • Marykwas, D.L.1    Schmidt, S.A.2    Berg, H.C.3
  • 29
    • 0033797058 scopus 로고    scopus 로고
    • Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS
    • J.M. Nieto, C. Madrid, A. Prenafeta, E. Miquelay, C. Balsalobre, M. Carrascal, and A. Juárez Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS Mol. Gen. Genet. 263 2000 349 358
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 349-358
    • Nieto, J.M.1    Madrid, C.2    Prenafeta, A.3    Miquelay, E.4    Balsalobre, C.5    Carrascal, M.6    Juárez, A.7
  • 32
    • 0036723747 scopus 로고    scopus 로고
    • Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin
    • C. Madrid, J.M. Nieto, S. Paytubi, M. Falconi, C.O. Gualerzi, and A. Juárez Temperature- and H-NS-dependent regulation of a plasmid-encoded virulence operon expressing Escherichia coli hemolysin J. Bacteriol. 184 2002 5058 5066
    • (2002) J. Bacteriol. , vol.184 , pp. 5058-5066
    • Madrid, C.1    Nieto, J.M.2    Paytubi, S.3    Falconi, M.4    Gualerzi, C.O.5    Juárez, A.6
  • 33
    • 0036174055 scopus 로고    scopus 로고
    • Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins
    • J.M. Nieto, C. Madrid, E. Miquelay, J.L. Parra, S. Rodríguez, and A. Juárez Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins J. Bacteriol. 184 2002 629 635
    • (2002) J. Bacteriol. , vol.184 , pp. 629-635
    • Nieto, J.M.1    Madrid, C.2    Miquelay, E.3    Parra, J.L.4    Rodríguez, S.5    Juárez, A.6
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemnli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 45 57
    • (1970) Nature , vol.227 , pp. 45-57
    • Laemnli, U.K.1
  • 37
    • 0027874398 scopus 로고
    • Protein chemical methods for molecular biologists
    • L.C. Packman Protein chemical methods for molecular biologists Methods Mol. Cell. Biol. 4 1993 189 198
    • (1993) Methods Mol. Cell. Biol. , vol.4 , pp. 189-198
    • Packman, L.C.1
  • 38
    • 0034695425 scopus 로고    scopus 로고
    • HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria
    • K.S. Gajiwala, and S.K. Burley HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria J. Mol. Biol. 295 2000 605 612
    • (2000) J. Mol. Biol. , vol.295 , pp. 605-612
    • Gajiwala, K.S.1    Burley, S.K.2
  • 39
    • 0027374131 scopus 로고
    • Physical map location of a set of Escherichia coli genes (hde) whose expression is affected by the nucleoid protein H-NS
    • T. Yoshida, C. Ueguchi, and T. Mizuno Physical map location of a set of Escherichia coli genes (hde) whose expression is affected by the nucleoid protein H-NS J. Bacteriol. 175 1993 7747 7748
    • (1993) J. Bacteriol. , vol.175 , pp. 7747-7748
    • Yoshida, T.1    Ueguchi, C.2    Mizuno, T.3
  • 40
    • 0027447019 scopus 로고
    • Function of the Escherichia coli nucleoid protein, H-NS: Molecular analysis of a subset of proteins whose expression is enhanced in an hns deletion mutant
    • T. Yoshida, C. Ueguchi, H. Yamada, and T. Mizuno Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in an hns deletion mutant Mol. Gen. Genet. 237 1993 113 122
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 113-122
    • Yoshida, T.1    Ueguchi, C.2    Yamada, H.3    Mizuno, T.4
  • 41
    • 0028920231 scopus 로고
    • The rpoE gene encoding the sigma e (sigma 24) heat shock sigma factor of Escherichia coli
    • S. Raina, D. Missiakas, and C. Georgopoulos The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli EMBO J. 14 1995 1043 1055
    • (1995) EMBO J. , vol.14 , pp. 1043-1055
    • Raina, S.1    Missiakas, D.2    Georgopoulos, C.3
  • 42
  • 43
    • 16544364071 scopus 로고    scopus 로고
    • The htrA (degP) gene of Listeria monocytogenes 10403S is essential for optimal growth under stress conditions
    • L.D. Wonderling, B.J. Wilkinson, and D.O. Bayles The htrA (degP) gene of Listeria monocytogenes 10403S is essential for optimal growth under stress conditions Appl. Environ. Microbiol. 70 2004 1935 1943
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1935-1943
    • Wonderling, L.D.1    Wilkinson, B.J.2    Bayles, D.O.3
  • 44
    • 0019508392 scopus 로고
    • Determination of the functions of haemolytic plasmid pHly152 of Escherichia coli
    • A. Noegel, U. Rdest, and W. Goebel Determination of the functions of haemolytic plasmid pHly152 of Escherichia coli J. Bacteriol. 145 1981 233 247
    • (1981) J. Bacteriol. , vol.145 , pp. 233-247
    • Noegel, A.1    Rdest, U.2    Goebel, W.3
  • 45
    • 0031757173 scopus 로고    scopus 로고
    • H-NS and StpA proteins stimulate expression of maltose regulon in Escherichia coli
    • J. Johansson, B. Dagberg, E. Richet, and B.E. Uhlin H-NS and StpA proteins stimulate expression of maltose regulon in Escherichia coli J. Bacteriol. 180 1998 6117 6125
    • (1998) J. Bacteriol. , vol.180 , pp. 6117-6125
    • Johansson, J.1    Dagberg, B.2    Richet, E.3    Uhlin, B.E.4


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