메뉴 건너뛰기




Volumn 158, Issue 6, 2007, Pages 529-536

The ompW (porin) gene mediates methyl viologen (paraquat) efflux in Salmonella enterica serovar Typhimurium

Author keywords

Methyl viologen; OmpW; Porin; Salmonella typhimurium

Indexed keywords

MEMBRANE PROTEIN; MESSENGER RNA; PARAQUAT; PORIN; PROTEIN OMPW; UNCLASSIFIED DRUG;

EID: 34547498442     PISSN: 09232508     EISSN: 17697123     Source Type: Journal    
DOI: 10.1016/j.resmic.2007.05.004     Document Type: Article
Times cited : (55)

References (31)
  • 1
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • Arora A., Rinehart D., Szabo G., and Tamm L.K. Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J. Biol. Chem. 275 (2000) 1594-1600
    • (2000) J. Biol. Chem. , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 2
    • 0013902668 scopus 로고
    • Antibiotic susceptibility testing by a standardized single disk method
    • Bauer A.W., Kirby W.M., Sherris J.C., and Turck M. Antibiotic susceptibility testing by a standardized single disk method. Am. J. Clin. Pathol. 45 (1966) 493-496
    • (1966) Am. J. Clin. Pathol. , vol.45 , pp. 493-496
    • Bauer, A.W.1    Kirby, W.M.2    Sherris, J.C.3    Turck, M.4
  • 3
    • 24944512361 scopus 로고    scopus 로고
    • Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae
    • Bisweswar N., Nandy R.K., Sarkar A., and Ghose A.C. Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae. Microbiology 151 (2005) 2975-2986
    • (2005) Microbiology , vol.151 , pp. 2975-2986
    • Bisweswar, N.1    Nandy, R.K.2    Sarkar, A.3    Ghose, A.C.4
  • 4
    • 33744502666 scopus 로고    scopus 로고
    • The cotranscribed Salmonella enterica sv. Typhi tsx and impX genes encode opposing nucleoside-specific import and export proteins
    • Bucarey S.A., Villagra N.A., Fuentes J.A., and Mora G.C. The cotranscribed Salmonella enterica sv. Typhi tsx and impX genes encode opposing nucleoside-specific import and export proteins. Genetics 173 (2006) 1-10
    • (2006) Genetics , vol.173 , pp. 1-10
    • Bucarey, S.A.1    Villagra, N.A.2    Fuentes, J.A.3    Mora, G.C.4
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes of Escherichia coli K-12 using PCR products
    • Datsenko K.A., and Wanner B.L. One-step inactivation of chromosomal genes of Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97 (2000) 6640-6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 0027386075 scopus 로고
    • Metabolism of dibenzothiopheno and naphtalene in Pseudomona strains: complete DNA sequence of an upper naphtalene catabolic pathway
    • Denome S.A., Stanley D.C., Olson E.S., and Young K.D. Metabolism of dibenzothiopheno and naphtalene in Pseudomona strains: complete DNA sequence of an upper naphtalene catabolic pathway. J. Bacteriol. 175 (1993) 6890-6901
    • (1993) J. Bacteriol. , vol.175 , pp. 6890-6901
    • Denome, S.A.1    Stanley, D.C.2    Olson, E.S.3    Young, K.D.4
  • 7
    • 0037094370 scopus 로고    scopus 로고
    • Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria
    • Ellermeier C.D., Janakiraman A., and Slauch J.M. Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria. Gene 290 (2002) 153-161
    • (2002) Gene , vol.290 , pp. 153-161
    • Ellermeier, C.D.1    Janakiraman, A.2    Slauch, J.M.3
  • 8
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical
    • Hassan H.M., and Fridovich I. Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J. Biol. Chem. 254 (1979) 10846-10852
    • (1979) J. Biol. Chem. , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 9
    • 8644260716 scopus 로고    scopus 로고
    • Analysis of TNT (2,4,6-trinitrotoluene)-inducible cellular responses and stress shock proteome in Stenotrophomonas sp. OK-5
    • Ho E.M., Chang H.W., Kim S.I., Kahng H.Y., and Oh K.H. Analysis of TNT (2,4,6-trinitrotoluene)-inducible cellular responses and stress shock proteome in Stenotrophomonas sp. OK-5. Curr. Microbiol. 49 (2004) 346-352
    • (2004) Curr. Microbiol. , vol.49 , pp. 346-352
    • Ho, E.M.1    Chang, H.W.2    Kim, S.I.3    Kahng, H.Y.4    Oh, K.H.5
  • 10
    • 33645779427 scopus 로고    scopus 로고
    • The outer membrane protein OmpW forms an eight-stranded β-barrel with a hydrophobic channel
    • Hong H., Patel D., Tamm L.K., and van der Berg B. The outer membrane protein OmpW forms an eight-stranded β-barrel with a hydrophobic channel. J. Biol. Chem. 281 (2006) 7568-7577
    • (2006) J. Biol. Chem. , vol.281 , pp. 7568-7577
    • Hong, H.1    Patel, D.2    Tamm, L.K.3    van der Berg, B.4
  • 12
    • 0025359644 scopus 로고
    • Nucleotide sequence of the gene, ompW, encoding a 22 kDa immunogenic outer membrane protein of Vibrio cholerae
    • Jalajakumari M.B., and Manning P.A. Nucleotide sequence of the gene, ompW, encoding a 22 kDa immunogenic outer membrane protein of Vibrio cholerae. Nucleic Acids Res. 18 (1990) 2180
    • (1990) Nucleic Acids Res. , vol.18 , pp. 2180
    • Jalajakumari, M.B.1    Manning, P.A.2
  • 13
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: barrels in a nutshell
    • Koebnik R., Locher K.P., and Van Gelder P. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37 (2000) 239-253
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 14
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller J.H. Experiments in Molecular Genetics (1972), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 15
    • 0023881454 scopus 로고
    • Isolation and characterization of methyl viologen-sensitive mutans of Escherichia coli K-12
    • Morimyo M. Isolation and characterization of methyl viologen-sensitive mutans of Escherichia coli K-12. J. Bacteriol. 170 (1988) 2136-2142
    • (1988) J. Bacteriol. , vol.170 , pp. 2136-2142
    • Morimyo, M.1
  • 16
    • 24944512361 scopus 로고    scopus 로고
    • Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae
    • Nandi B., Nandy R.K., Sarkar A., and Ghose A.C. Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae. Microbiology 151 (2005) 2975-2986
    • (2005) Microbiology , vol.151 , pp. 2975-2986
    • Nandi, B.1    Nandy, R.K.2    Sarkar, A.3    Ghose, A.C.4
  • 17
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido H. Multidrug efflux pumps of gram-negative bacteria. J. Bacteriol. 178 (1996) 5853-5859
    • (1996) J. Bacteriol. , vol.178 , pp. 5853-5859
    • Nikaido, H.1
  • 18
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67 (2003) 593-656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 21
    • 0033000807 scopus 로고    scopus 로고
    • Characterization of colicin S4 and its receptor OmpW, a minor protein of Escherichia coli outer membrane
    • Pilsl H., Smajs D., and Braun V. Characterization of colicin S4 and its receptor OmpW, a minor protein of Escherichia coli outer membrane. J. Bacteriol. 181 (1999) 3578-3581
    • (1999) J. Bacteriol. , vol.181 , pp. 3578-3581
    • Pilsl, H.1    Smajs, D.2    Braun, V.3
  • 24
    • 0036437016 scopus 로고    scopus 로고
    • The Salmonella enterica serovar Typhimurium smvA, yddG and ompD (porin) genes are required for the efficient efflux of methyl viologen
    • Santiviago C.A., Fuentes J.A., Bueno S.M., Trombert N., Hidalgo A.A., Socias L.T., Youderian P., and Mora G. The Salmonella enterica serovar Typhimurium smvA, yddG and ompD (porin) genes are required for the efficient efflux of methyl viologen. Mol. Microbiol. 46 (2002) 687-698
    • (2002) Mol. Microbiol. , vol.46 , pp. 687-698
    • Santiviago, C.A.1    Fuentes, J.A.2    Bueno, S.M.3    Trombert, N.4    Hidalgo, A.A.5    Socias, L.T.6    Youderian, P.7    Mora, G.8
  • 25
    • 27844581259 scopus 로고    scopus 로고
    • Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli
    • Semchyshyn H., Bagnyukova T., Storey K., and Lushchak V. Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli. Cell Biol. Intern. 29 (2005) 898-902
    • (2005) Cell Biol. Intern. , vol.29 , pp. 898-902
    • Semchyshyn, H.1    Bagnyukova, T.2    Storey, K.3    Lushchak, V.4
  • 26
    • 0026785288 scopus 로고
    • Pore-forming activity of OmpA protein of Escherichia coli
    • Sugawara E., and Nikaido H. Pore-forming activity of OmpA protein of Escherichia coli. J. Biol. Chem. 267 (1992) 2507-2511
    • (1992) J. Biol. Chem. , vol.267 , pp. 2507-2511
    • Sugawara, E.1    Nikaido, H.2
  • 28
    • 0034969905 scopus 로고    scopus 로고
    • Analysis of Pseudomonas putida alkane-degradation gene clusters and flanking insertion sequences. Evolution and regulation of the alk genes
    • van Beilen J., Panke S., Franchini A., Rothlisberger M., and Withol B. Analysis of Pseudomonas putida alkane-degradation gene clusters and flanking insertion sequences. Evolution and regulation of the alk genes. Microbiology 147 (2001) 1621-1630
    • (2001) Microbiology , vol.147 , pp. 1621-1630
    • van Beilen, J.1    Panke, S.2    Franchini, A.3    Rothlisberger, M.4    Withol, B.5
  • 29
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang Y. The function of OmpA in Escherichia coli. Biochem. Biophys. Res. Commun. 292 (2002) 396-401
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 396-401
    • Wang, Y.1
  • 30
    • 0032702739 scopus 로고    scopus 로고
    • Interdependence of the position and orientation of SoxS binding sites in the transcriptional activation of the class I subset of Escherichia coli superoxide-inducible promoters
    • Wood T.I., Griffith K.L., Fawcett W.P., Jair K.W., Schneider T.D., and Wolf Jr. R.E. Interdependence of the position and orientation of SoxS binding sites in the transcriptional activation of the class I subset of Escherichia coli superoxide-inducible promoters. Mol. Microbiol. 34 (1999) 414-430
    • (1999) Mol. Microbiol. , vol.34 , pp. 414-430
    • Wood, T.I.1    Griffith, K.L.2    Fawcett, W.P.3    Jair, K.W.4    Schneider, T.D.5    Wolf Jr., R.E.6
  • 31
    • 23844521625 scopus 로고    scopus 로고
    • Protein analysis on the expression of outer membrane proteins of Vibrio alginolyticus at different sodium concentrations
    • Xu C., Wang S., Ren H., Lin X., and Wu L. Protein analysis on the expression of outer membrane proteins of Vibrio alginolyticus at different sodium concentrations. Proteomics 5 (2005) 3142-3152
    • (2005) Proteomics , vol.5 , pp. 3142-3152
    • Xu, C.1    Wang, S.2    Ren, H.3    Lin, X.4    Wu, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.