메뉴 건너뛰기




Volumn 191, Issue 3, 2009, Pages 898-908

Analysis of secretin-induced stress in Pseudomonas aeruginosa suggests prevention rather than response and identifies a novel protein involved in secretin function

Author keywords

[No Author keywords available]

Indexed keywords

PERIPLASMIC PROTEIN; PROTEIN; PROTEIN TRUB; PROTEIN XCPQ; SECRETIN; SIGMA FACTOR RPON; UNCLASSIFIED DRUG; ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; MEMBRANE PROTEIN; XCPQ PROTEIN, PSEUDOMONAS AERUGINOSA;

EID: 63449111011     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01443-08     Document Type: Article
Times cited : (26)

References (58)
  • 1
    • 0036173113 scopus 로고    scopus 로고
    • A novel type II secretion system in Pseudomonas aeruginosa
    • Ball, G., E. Durand, A. Lazdunski, and A. Filloux. 2002. A novel type II secretion system in Pseudomonas aeruginosa. Mol. Microbiol. 43:475-485.
    • (2002) Mol. Microbiol , vol.43 , pp. 475-485
    • Ball, G.1    Durand, E.2    Lazdunski, A.3    Filloux, A.4
  • 3
    • 0037615052 scopus 로고    scopus 로고
    • Secretins of Pseudomonas aeruginosa: Large holes in the outer membrane
    • Bitter, W. 2003. Secretins of Pseudomonas aeruginosa: large holes in the outer membrane. Arch. Microbiol. 179:307-314.
    • (2003) Arch. Microbiol , vol.179 , pp. 307-314
    • Bitter, W.1
  • 4
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aemginosa
    • Bitter, W., M. Koster, M. Latijnhouwers, H. de Cock, and J. Tommassen. 1998. Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aemginosa. Mol. Microbiol. 27:209-219.
    • (1998) Mol. Microbiol , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    de Cock, H.4    Tommassen, J.5
  • 5
    • 34247890081 scopus 로고    scopus 로고
    • Species-specific functioning of the Pseudomonas XcpQ secretin: Role for the C-terminal homology domain and lipopolysaccharide
    • Bitter, W., R. van Boxtel, M. Groeneweg, P. S. Carballo, U. Zahringer, J. Tommassen, and M. Koster. 2007. Species-specific functioning of the Pseudomonas XcpQ secretin: role for the C-terminal homology domain and lipopolysaccharide. J. Bacteriol. 189:2967-2975.
    • (2007) J. Bacteriol , vol.189 , pp. 2967-2975
    • Bitter, W.1    van Boxtel, R.2    Groeneweg, M.3    Carballo, P.S.4    Zahringer, U.5    Tommassen, J.6    Koster, M.7
  • 8
    • 0014874110 scopus 로고
    • Release of alkaline phosphatase from cells of Pseudomonas aemginosa by manipulation of cation concentration and of pH
    • Cheng, K. J., J. M. Ingram, and J. W. Costerton. 1970. Release of alkaline phosphatase from cells of Pseudomonas aemginosa by manipulation of cation concentration and of pH. J. Bacteriol. 104:748-753.
    • (1970) J. Bacteriol , vol.104 , pp. 748-753
    • Cheng, K.J.1    Ingram, J.M.2    Costerton, J.W.3
  • 9
    • 32244448730 scopus 로고    scopus 로고
    • A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: Application for DNA fragment transfer between chromosomes and plasmid transformation
    • Choi, K. H., A. Kumar, and H. P. Schweizer. 2006. A 10-min method for preparation of highly electrocompetent Pseudomonas aeruginosa cells: application for DNA fragment transfer between chromosomes and plasmid transformation. J. Microbiol. Methods 64:391-397.
    • (2006) J. Microbiol. Methods , vol.64 , pp. 391-397
    • Choi, K.H.1    Kumar, A.2    Schweizer, H.P.3
  • 10
    • 22644441730 scopus 로고    scopus 로고
    • The phage-shock-protein response
    • Darwin, A. J. 2005. The phage-shock-protein response. Mol. Microbiol. 57:621-628.
    • (2005) Mol. Microbiol , vol.57 , pp. 621-628
    • Darwin, A.J.1
  • 11
    • 0035154988 scopus 로고    scopus 로고
    • The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced
    • Darwin, A. J., and V. L. Miller. 2001. The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced. Mol. Microbiol. 39:429-444.
    • (2001) Mol. Microbiol , vol.39 , pp. 429-444
    • Darwin, A.J.1    Miller, V.L.2
  • 12
  • 13
    • 33646072467 scopus 로고    scopus 로고
    • The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?
    • Dorel, C., P. Lejeune, and A. Rodrigue, 2006. The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities? Res. Microbiol. 157:306-314.
    • (2006) Res. Microbiol , vol.157 , pp. 306-314
    • Dorel, C.1    Lejeune, P.2    Rodrigue, A.3
  • 14
    • 0031754788 scopus 로고    scopus 로고
    • GSP-dependent protein secretion in gram-negative bacteria: The Xcp system of Pseudomonas aeruginosa
    • Filloux, A., G. Michel, and M. Bally. 1998. GSP-dependent protein secretion in gram-negative bacteria: the Xcp system of Pseudomonas aeruginosa. FEMS Microbiol. Rev. 22:177-198.
    • (1998) FEMS Microbiol. Rev , vol.22 , pp. 177-198
    • Filloux, A.1    Michel, G.2    Bally, M.3
  • 15
    • 0023097732 scopus 로고
    • Characterization of two Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants
    • Filloux, A., M. Murgier, B. Wretlind, and A. Lazdunski. 1987. Characterization of two Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants. FEMS Microbiol. Lett. 40:159-163.
    • (1987) FEMS Microbiol. Lett , vol.40 , pp. 159-163
    • Filloux, A.1    Murgier, M.2    Wretlind, B.3    Lazdunski, A.4
  • 16
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin, S., and C. A. Boucher. 1994. A superfamily of proteins involved in different secretion pathways in gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol. Gen. Genet. 243:112-118.
    • (1994) Mol. Gen. Genet , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 17
    • 7744220530 scopus 로고    scopus 로고
    • A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa
    • Goodman, A. L., B. Kulasekara, A. Rietsch, D. Boyd, R. S. Smith, and S. Lory. 2004. A signaling network reciprocally regulates genes associated with acute infection and chronic persistence in Pseudomonas aeruginosa. Dev. Cell 7:745-754.
    • (2004) Dev. Cell , vol.7 , pp. 745-754
    • Goodman, A.L.1    Kulasekara, B.2    Rietsch, A.3    Boyd, D.4    Smith, R.S.5    Lory, S.6
  • 18
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout, I., M. Chami, A. Engel, A. P. Pugsley, and N. Bayan. 2006. Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J. 25:5241-5249.
    • (2006) EMBO J , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 19
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K. R., S. Lory, and A. P. Pugsley. 1996. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15:978-988.
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 20
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: Separation of proteolytic protection and piloting functions
    • Hardie, K. R., A. Seydel, L Guilvout, and A. P. Pugsley. 1996. The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol. Microbiol. 22:967-976.
    • (1996) Mol. Microbiol , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, L.3    Pugsley, A.P.4
  • 21
    • 33646795317 scopus 로고    scopus 로고
    • Biofilm formation by Pseudomonas fluorescens WCS365: A role for LapD
    • Hinsa, S. M., and G. A. O'Toole. 2006. Biofilm formation by Pseudomonas fluorescens WCS365: a role for LapD. Microbiology 152:1375-1383.
    • (2006) Microbiology , vol.152 , pp. 1375-1383
    • Hinsa, S.M.1    O'Toole, G.A.2
  • 22
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: Application for isolation of unmarked Pseudomonas aemginosa mutants
    • Hoang, T. T., R. R. Karkhoff-Schweizer, A. J. Kutchma, and H. P. Schweizer. 1998. A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aemginosa mutants. Gene 212:77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 23
    • 0033968474 scopus 로고    scopus 로고
    • Integration-proficient plasmids for Pseudomonas aeruginosa: Site-specific integration and use for engineering of reporter and expression strains
    • Hoang, T. T., A. J. Kutchma, A. Becher, and H. P. Schweizer. 2000. Integration-proficient plasmids for Pseudomonas aeruginosa: site-specific integration and use for engineering of reporter and expression strains. Plasmid 43:59-72.
    • (2000) Plasmid , vol.43 , pp. 59-72
    • Hoang, T.T.1    Kutchma, A.J.2    Becher, A.3    Schweizer, H.P.4
  • 24
    • 0030028862 scopus 로고    scopus 로고
    • Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions
    • Kleerebezem, M., W. Crielaard, and J. Tommassen. 1996. Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions. EMBO. J. 15:162-171.
    • (1996) EMBO. J , vol.15 , pp. 162-171
    • Kleerebezem, M.1    Crielaard, W.2    Tommassen, J.3
  • 25
    • 55749114256 scopus 로고    scopus 로고
    • PilF is an outer membrane lipoprotein required for multi-merization and localization of the Pseudomonas aeruginosa type IV pilus secretin
    • Koo, J., S. Tammam, S. Y. Ku, L. Sampaleanu, L. L. Burrows, and P. L. Howell. 2008. PilF is an outer membrane lipoprotein required for multi-merization and localization of the Pseudomonas aeruginosa type IV pilus secretin. J. Bacteriol. 190:6961-6969.
    • (2008) J. Bacteriol , vol.190 , pp. 6961-6969
    • Koo, J.1    Tammam, S.2    Ku, S.Y.3    Sampaleanu, L.4    Burrows, L.L.5    Howell, P.L.6
  • 26
    • 14644388889 scopus 로고    scopus 로고
    • Genome-wide identification of Pseudomonas aemginosa exported proteins using a consensus computational strategy combined with a laboratory-based PhoA fusion screen
    • Lewenza, S., J. L. Gardy, F. S. Brinkman, and R. E. Hancock. 2005. Genome-wide identification of Pseudomonas aemginosa exported proteins using a consensus computational strategy combined with a laboratory-based PhoA fusion screen. Genome Res. 15:321-329.
    • (2005) Genome Res , vol.15 , pp. 321-329
    • Lewenza, S.1    Gardy, J.L.2    Brinkman, F.S.3    Hancock, R.E.4
  • 27
    • 11244353225 scopus 로고    scopus 로고
    • Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG)
    • Lloyd, L. J., S. E. Jones, G. Jovanovic, P. Gyaneshwar, M. D. Rolfe, A. Thompson, J. C. Hinton, and M. Buck. 2004. Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG). J. Biol. Chem. 279:55707-55714.
    • (2004) J. Biol. Chem , vol.279 , pp. 55707-55714
    • Lloyd, L.J.1    Jones, S.E.2    Jovanovic, G.3    Gyaneshwar, P.4    Rolfe, M.D.5    Thompson, A.6    Hinton, J.C.7    Buck, M.8
  • 28
    • 34547645814 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa secreted protein PA2934 decreases apical membrane expression of the cystic fibrosis transmembrane conductance regulator
    • MacEachran, D. P., S. Ye, J. M. Bomberger, D. A. Hogan, A. Swiatecka-Urban, B. A. Stanton, and G. A. O'Toole. 2007. The Pseudomonas aeruginosa secreted protein PA2934 decreases apical membrane expression of the cystic fibrosis transmembrane conductance regulator. Infect. Immun. 75:3902-3912.
    • (2007) Infect. Immun , vol.75 , pp. 3902-3912
    • MacEachran, D.P.1    Ye, S.2    Bomberger, J.M.3    Hogan, D.A.4    Swiatecka-Urban, A.5    Stanton, B.A.6    O'Toole, G.A.7
  • 29
    • 0027235766 scopus 로고
    • Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa
    • Martin, P. R., M. Hobbs, P. D. Free, Y. Jeske, and J. S. Mattick. 1993. Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa. Mol. Microbiol. 9:857-868.
    • (1993) Mol. Microbiol , vol.9 , pp. 857-868
    • Martin, P.R.1    Hobbs, M.2    Free, P.D.3    Jeske, Y.4    Mattick, J.S.5
  • 30
    • 0031776687 scopus 로고    scopus 로고
    • Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion
    • Martinez, A., P. Ostrovsky, and D. N. Nunn. 1998. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28:1235-1246.
    • (1998) Mol. Microbiol , vol.28 , pp. 1235-1246
    • Martinez, A.1    Ostrovsky, P.2    Nunn, D.N.3
  • 31
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama, S., T. Tajima, and H. Tokuda. 1995. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J. 14:3365-3372.
    • (1995) EMBO J , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 32
    • 3042513855 scopus 로고    scopus 로고
    • Identification of inducers of the Yersinia enterocolitica phage shock protein system and comparison to the regulation of the RpoE and Cpx extracytoplasmic stress responses
    • Maxson, M. E., and A. J. Darwin. 2004. Identification of inducers of the Yersinia enterocolitica phage shock protein system and comparison to the regulation of the RpoE and Cpx extracytoplasmic stress responses. J. Bacteriol. 186:4199-208.
    • (2004) J. Bacteriol , vol.186 , pp. 4199-4208
    • Maxson, M.E.1    Darwin, A.J.2
  • 33
    • 33645072461 scopus 로고    scopus 로고
    • PspB and PspC of Yersinia enterocolitica are dual function proteins: Regulators and effectors of the phage-shock-protein response
    • Maxson, M. E., and A. J. Darwin. 2006. PspB and PspC of Yersinia enterocolitica are dual function proteins: regulators and effectors of the phage-shock-protein response. Mol. Microbiol. 59:1610-1623.
    • (2006) Mol. Microbiol , vol.59 , pp. 1610-1623
    • Maxson, M.E.1    Darwin, A.J.2
  • 34
    • 0033958457 scopus 로고    scopus 로고
    • Alteration of the lipopolysaccharide structure affects the functioning of the Xcp secretory system in Pseudomonas aeruginosa
    • Michel, G., G. Ball, J. B. Goldberg, and A. Lazdunski. 2000. Alteration of the lipopolysaccharide structure affects the functioning of the Xcp secretory system in Pseudomonas aeruginosa. J. Bacteriol. 182:696-703.
    • (2000) J. Bacteriol , vol.182 , pp. 696-703
    • Michel, G.1    Ball, G.2    Goldberg, J.B.3    Lazdunski, A.4
  • 35
    • 34248402363 scopus 로고    scopus 로고
    • XphA/XqhA, a novel GspCD subunit for type II secretion in Pseudomonas aeruginosa
    • Michel, G. P., E. Durand, and A. Filloux. 2007. XphA/XqhA, a novel GspCD subunit for type II secretion in Pseudomonas aeruginosa. J. Bacteriol. 189: 3776-3783.
    • (2007) J. Bacteriol , vol.189 , pp. 3776-3783
    • Michel, G.P.1    Durand, E.2    Filloux, A.3
  • 37
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170:2575-2583.
    • (1988) J. Bacteriol , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 38
    • 0030907620 scopus 로고    scopus 로고
    • The Escherichia coli phage-shock-protein (psp) Operon
    • Model, P., G. Jovanovic, and J. Dworkin. 1997. The Escherichia coli phage-shock-protein (psp) Operon. Mol. Microbiol. 24:255-261.
    • (1997) Mol. Microbiol , vol.24 , pp. 255-261
    • Model, P.1    Jovanovic, G.2    Dworkin, J.3
  • 39
    • 0033580277 scopus 로고    scopus 로고
    • Broad-host-range expression vectors that cany the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator
    • Newman, J. R., and C. Fuqua. 1999. Broad-host-range expression vectors that cany the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator. Gene 227:197-203.
    • (1999) Gene , vol.227 , pp. 197-203
    • Newman, J.R.1    Fuqua, C.2
  • 40
    • 0038486028 scopus 로고    scopus 로고
    • Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1
    • Nouwens, A. S., S. A. Beatson, C. B. Whitchurch, B. J. Walsh, H. P. Schweizer, J. S. Mattick, and S. J. Cordwell. 2003. Proteome analysis of extracellular proteins regulated by the las and rhl quorum sensing systems in Pseudomonas aeruginosa PAO1. Microbiology 149:1311-1322.
    • (2003) Microbiology , vol.149 , pp. 1311-1322
    • Nouwens, A.S.1    Beatson, S.A.2    Whitchurch, C.B.3    Walsh, B.J.4    Schweizer, H.P.5    Mattick, J.S.6    Cordwell, S.J.7
  • 41
    • 0027273016 scopus 로고    scopus 로고
    • Nunn, D. N., and S. Lory. 1993. Cleavage, methylation. and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W. J. Bacteriol. 175:4375-382.
    • Nunn, D. N., and S. Lory. 1993. Cleavage, methylation. and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W. J. Bacteriol. 175:4375-382.
  • 43
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: A genetic analysis
    • O'Toole, G. A., and R. Kolter. 1998. Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis. Mol. Microbiol. 28:449-161.
    • (1998) Mol. Microbiol , vol.28 , pp. 449-161
    • O'Toole, G.A.1    Kolter, R.2
  • 45
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio, T. L. 2005. Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56:1119-1128.
    • (2005) Mol. Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 46
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • Raivio, T. L., and T. J. Silhavy. 2001. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:591-624.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 47
    • 0033106492 scopus 로고    scopus 로고
    • E and Cpx regulatory pathways: Overlapping but distinct envelope stress responses
    • E and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr. Opin. Microbiol. 2:159-165.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 48
    • 33646851752 scopus 로고    scopus 로고
    • Pushing the envelope: Extracytoplasmie stress responses in bacterial pathogens
    • Rowley, G., M. Spector, J. Kormanec, and M, Roberts. 2006. Pushing the envelope: extracytoplasmie stress responses in bacterial pathogens. Nat. Rev. Microbiol. 4:383-394.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 383-394
    • Rowley, G.1    Spector, M.2    Kormanec, J.3    Roberts, M.4
  • 49
    • 0031032631 scopus 로고    scopus 로고
    • Molecular characterization of mutants affected in the osmoprotectant-dependent induction of phospho-lipase C in Pseudomonas aeruginosa PAOl
    • Sage, A. E., A. I, Vasil, and M. L, Vasil. 1997. Molecular characterization of mutants affected in the osmoprotectant-dependent induction of phospho-lipase C in Pseudomonas aeruginosa PAOl. Mol. Microbiol. 23:43-56.
    • (1997) Mol. Microbiol , vol.23 , pp. 43-56
    • Sage, A.E.A.I.1    Vasil2    Vasil, M.L.3
  • 50
    • 34447556822 scopus 로고    scopus 로고
    • Global analysis of tolerance to se cretin-induced stress in Yersinia enterocolitica suggests that the phage-shock-protein system may be a remarkably self-contained stress response
    • Seo, J., D. C. Savitzky, E. Ford, and A, J. Darwin. 2007. Global analysis of tolerance to se cretin-induced stress in Yersinia enterocolitica suggests that the phage-shock-protein system may be a remarkably self-contained stress response. Mol. Microbiol. 65:714-727.
    • (2007) Mol. Microbiol , vol.65 , pp. 714-727
    • Seo, J.1    Savitzky, D.C.2    Ford, E.3    Darwin, A.J.4
  • 51
    • 0022536054 scopus 로고
    • Cloning and expression of the pilin gene of Pseudomonas aeruginosa PAK in Escherichia coli
    • Strom, M. S., and S. Lory. 1986. Cloning and expression of the pilin gene of Pseudomonas aeruginosa PAK in Escherichia coli. J. Bacteriol. 165:367-372.
    • (1986) J. Bacteriol , vol.165 , pp. 367-372
    • Strom, M.S.1    Lory, S.2
  • 53
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux, R., G. Ball, B. Ize, M. L. Vasil, A. Lazdunski, L. F. Wu, and A. Filloux. 2001. Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20:6735-6741.
    • (2001) EMBO J , vol.20 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Filloux, A.7
  • 54
    • 0037322193 scopus 로고    scopus 로고
    • Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway
    • Wolfgang, M. C., V. T. Lee, M. E. Gilmore, and S. Lory. 2003. Coordinate regulation of bacterial virulence genes by a novel adenylate cyclase-dependent signaling pathway. Dev. Cell 4:253-263.
    • (2003) Dev. Cell , vol.4 , pp. 253-263
    • Wolfgang, M.C.1    Lee, V.T.2    Gilmore, M.E.3    Lory, S.4
  • 56
    • 0024401938 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein F: Structural role and relationship to the Escherichia coli OmpA protein
    • Woodruff, W. A., and R. E. Hancock. 1989. Pseudomonas aeruginosa outer membrane protein F: structural role and relationship to the Escherichia coli OmpA protein. J. Bacteriol. 171:3304-3309.
    • (1989) J. Bacteriol , vol.171 , pp. 3304-3309
    • Woodruff, W.A.1    Hancock, R.E.2
  • 57
    • 0029801248 scopus 로고    scopus 로고
    • Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway
    • Yahr, T. L., J. Goranson, and D.W. Frank. 1996. Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway. Mol. Microbiol. 22:991-1003.
    • (1996) Mol. Microbiol , vol.22 , pp. 991-1003
    • Yahr, T.L.1    Goranson, J.2    Frank, D.W.3
  • 58
    • 0030877188 scopus 로고    scopus 로고
    • Identification of novel chromosomal loci affecting Yersinia enterocolitica pathogenesis
    • Young, G. M., and V. L. Miller, 1997. Identification of novel chromosomal loci affecting Yersinia enterocolitica pathogenesis. Mol. Microbiol. 25:319-328.
    • (1997) Mol. Microbiol , vol.25 , pp. 319-328
    • Young, G.M.1    Miller, V.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.