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Volumn 181, Issue 3, 1999, Pages 791-798

Excretion of endogenous cadaverine leads to a decrease in porin-mediated outer membrane permeability

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; CADAVERINE; CEFALORIDINE; LYSINE; POLYAMINE; PORIN;

EID: 0032944380     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.3.791-798.1999     Document Type: Article
Times cited : (73)

References (43)
  • 1
    • 0024385329 scopus 로고
    • Construction of lac fusions to the inducible arginine and lysine decarboxylase genes of Escherichia coli K-12
    • Auger, E. P., K. E. Redding, T. Plumb, L. C. Childs, S.-Y. Meng, and G. N. Bennett. 1989. Construction of lac fusions to the inducible arginine and lysine decarboxylase genes of Escherichia coli K-12. Mol. Microbiol. 3:609-620.
    • (1989) Mol. Microbiol. , vol.3 , pp. 609-620
    • Auger, E.P.1    Redding, K.E.2    Plumb, T.3    Childs, L.C.4    Meng, S.-Y.5    Bennett, G.N.6
  • 2
    • 0344526031 scopus 로고    scopus 로고
    • Personal communication
    • Bennett, G. Personal communication.
    • Bennett, G.1
  • 3
    • 0024154771 scopus 로고
    • Structure and function of porins from gram-negative bacteria
    • Benz, R. 1988. Structure and function of porins from Gram-negative bacteria. Annu. Rev. Microbiol. 42:359-393.
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 359-393
    • Benz, R.1
  • 4
    • 0018617661 scopus 로고
    • Plasmids of Escherichia coli as cloning vectors
    • Bolivar, F., and K. Backman. 1979. Plasmids of Escherichia coli as cloning vectors. Methods Enzymol. 68:245-267.
    • (1979) Methods Enzymol. , vol.68 , pp. 245-267
    • Bolivar, F.1    Backman, K.2
  • 5
    • 0021884143 scopus 로고
    • Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope
    • Buch, J. K., and S. M. Boyle. 1985. Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope. J. Bacteriol. 163:522-527.
    • (1985) J. Bacteriol. , vol.163 , pp. 522-527
    • Buch, J.K.1    Boyle, S.M.2
  • 6
    • 0000182975 scopus 로고
    • XL1-blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W. O., J. M. Fernandez, and J. M. Short. 1987. XL1-blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTechniques 5:376-378.
    • (1987) BioTechniques , vol.5 , pp. 376-378
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 8
    • 0028828533 scopus 로고
    • Cadaverine induces closing of E. coli porins
    • delaVega, A. L., and A. H. Delcour. 1995. Cadaverine induces closing of E. coli porins. EMBO J. 14:6058-6065.
    • (1995) EMBO J. , vol.14 , pp. 6058-6065
    • DelaVega, A.L.1    Delcour, A.H.2
  • 9
    • 8944248272 scopus 로고    scopus 로고
    • Polyamines decrease Escherichia coli outer membrane permeability
    • delaVega, A. L., and A. H. Delcour. 1996. Polyamines decrease Escherichia coli outer membrane permeability. J. Bacteriol. 178:3715-3721.
    • (1996) J. Bacteriol. , vol.178 , pp. 3715-3721
    • DelaVega, A.L.1    Delcour, A.H.2
  • 10
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: Insights from electrophysiology
    • Delcour, A. H. 1997. Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol. Lett. 151:115-123.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 115-123
    • Delcour, A.H.1
  • 11
    • 0028004066 scopus 로고
    • Altered pH and lysine signalling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon
    • Dell, C. L., M. N. Neely, and E. R. Olson. 1994. Altered pH and lysine signalling mutants of cadC, a gene encoding a membrane-bound transcriptional activator of the Escherichia coli cadBA operon. Mol. Microbiol. 14:7-16.
    • (1994) Mol. Microbiol. , vol.14 , pp. 7-16
    • Dell, C.L.1    Neely, M.N.2    Olson, E.R.3
  • 13
    • 0024340114 scopus 로고
    • New method for generating deletions and gene replacements in Escherichia coli
    • Hamilton, C. M., M. Aldea, B. K. Washburn, P. Babitzke, and S. R. Kushner. 1989. New method for generating deletions and gene replacements in Escherichia coli. J. Bacteriol. 171:4617-4622.
    • (1989) J. Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 15
    • 0019814049 scopus 로고
    • Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin
    • Harder, K., H. Nikaido, and M. Matsuhashi. 1981. Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the ompF porin. Antimicrob. Agents Chemother. 20:549-552.
    • (1981) Antimicrob. Agents Chemother. , vol.20 , pp. 549-552
    • Harder, K.1    Nikaido, H.2    Matsuhashi, M.3
  • 16
    • 0015966516 scopus 로고
    • Molecular specificities of R factor-determined beta-lactamases: Correlation with plasmid compatibility
    • Hedges, R. W., N. Datta, P. Kontomichalou, and J. T. Smith. 1974. Molecular specificities of R factor-determined beta-lactamases: correlation with plasmid compatibility. J. Bacteriol. 117:56-62.
    • (1974) J. Bacteriol. , vol.117 , pp. 56-62
    • Hedges, R.W.1    Datta, N.2    Kontomichalou, P.3    Smith, J.T.4
  • 17
    • 0023374547 scopus 로고
    • Regulation of major outer membrane porin proteins of Escherichia coli K-12 by pH
    • Heyde, M., and R. Portalier. 1987. Regulation of major outer membrane porin proteins of Escherichia coli K-12 by pH. Mol. Gen. Genet. 208:511-517.
    • (1987) Mol. Gen. Genet. , vol.208 , pp. 511-517
    • Heyde, M.1    Portalier, R.2
  • 19
    • 0030956162 scopus 로고    scopus 로고
    • + channels: Evidence for a trap door mechanisms of activation gating
    • + channels: evidence for a trap door mechanisms of activation gating. J. Gen. Physiol. 109:527-535.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 527-535
    • Holmgren, M.1    Smith, P.L.2    Yellen, G.3
  • 20
    • 0025339191 scopus 로고
    • Effect of outer membrane permeability on chemotaxis in Escherichia coli
    • Ingham, C., M. Buechner, and J. Adler. 1990. Effect of outer membrane permeability on chemotaxis in Escherichia coli. J. Bacteriol. 172:3577-3583.
    • (1990) J. Bacteriol. , vol.172 , pp. 3577-3583
    • Ingham, C.1    Buechner, M.2    Adler, J.3
  • 21
    • 0030839791 scopus 로고    scopus 로고
    • Complex inhibition of OmpF and OmpC bacterial porins by polyamines
    • Iyer, R., and A. H. Delcour. 1997. Complex inhibition of OmpF and OmpC bacterial porins by polyamines. J. Biol. Chem. 272:18595-18601.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18595-18601
    • Iyer, R.1    Delcour, A.H.2
  • 23
    • 0030047530 scopus 로고    scopus 로고
    • Modulation of channel function by polyamines
    • Johnson, T. D. 1996. Modulation of channel function by polyamines. Trends Pharmacol. Sci. 17:22-27.
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 22-27
    • Johnson, T.D.1
  • 24
    • 0025720216 scopus 로고
    • Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome
    • Kashiwagi, K., T. Suzuki, F. Suzuki, T. Furuchi, H. Kobayashi, and K. Igarashi. 1991. Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome. J. Biol. Chem. 266:20922-20927.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20922-20927
    • Kashiwagi, K.1    Suzuki, T.2    Suzuki, F.3    Furuchi, T.4    Kobayashi, H.5    Igarashi, K.6
  • 26
    • 0025866196 scopus 로고
    • Polyamines as constituents of the outer membranes of Escherichia coli and Salmonella typhimurium
    • Koski, P., and M. Vaara. 1991. Polyamines as constituents of the outer membranes of Escherichia coli and Salmonella typhimurium. J. Bacteriol. 173:3695-3699.
    • (1991) J. Bacteriol. , vol.173 , pp. 3695-3699
    • Koski, P.1    Vaara, M.2
  • 27
    • 0031717824 scopus 로고    scopus 로고
    • Inhibitory effect of acidic pH on OmpC porin: Wildtype and mutant studies
    • Liu, N., and A. H. Delcour. 1998. Inhibitory effect of acidic pH on OmpC porin: wildtype and mutant studies. FEBS Lett. 434:160-164.
    • (1998) FEBS Lett. , vol.434 , pp. 160-164
    • Liu, N.1    Delcour, A.H.2
  • 28
    • 0027984375 scopus 로고
    • Potassium channel blocking by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • Lopatin, A., E. N. Makhina, and C. G. Nichols. 1994. Potassium channel blocking by cytoplasmic polyamines as the mechanism of intrinsic rectification. Nature 372:366-369.
    • (1994) Nature , vol.372 , pp. 366-369
    • Lopatin, A.1    Makhina, E.N.2    Nichols, C.G.3
  • 29
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH
    • Meng, S.-Y., and G. N. Bennett. 1992. Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pH. J. Bacteriol. 174:2659-2669.
    • (1992) J. Bacteriol. , vol.174 , pp. 2659-2669
    • Meng, S.-Y.1    Bennett, G.N.2
  • 30
    • 0026772549 scopus 로고
    • Regulation of the Escherichia coli cad operon: Location of a site required for acid induction
    • Meng, S. Y., and G. N. Bennett. 1992. Regulation of the Escherichia coli cad operon: location of a site required for acid induction. J. Bacteriol. 174:2670-2678.
    • (1992) J. Bacteriol. , vol.174 , pp. 2670-2678
    • Meng, S.Y.1    Bennett, G.N.2
  • 31
    • 0015522503 scopus 로고
    • Dependence of the putrescine content of Escherichia coli on the osmotic strength of the medium
    • Munro, G. F., K. Hercules, J. Morgan, and W. Sauerbier. 1972. Dependence of the putrescine content of Escherichia coli on the osmotic strength of the medium. J. Biol. Chem. 247:1272-1280.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1272-1280
    • Munro, G.F.1    Hercules, K.2    Morgan, J.3    Sauerbier, W.4
  • 32
    • 0028229613 scopus 로고
    • Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon
    • Neely, M. N., C. L. Dell, and E. R. Olson. 1994. Roles of LysP and CadC in mediating the lysine requirement for acid induction of the Escherichia coli cad operon. J. Bacteriol. 176:3278-3285.
    • (1994) J. Bacteriol. , vol.176 , pp. 3278-3285
    • Neely, M.N.1    Dell, C.L.2    Olson, E.R.3
  • 33
    • 0029812095 scopus 로고    scopus 로고
    • Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine
    • Neely, M. N., and E. R. Olson. 1996. Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysine. J. Bacteriol. 178:5522-5528.
    • (1996) J. Bacteriol. , vol.178 , pp. 5522-5528
    • Neely, M.N.1    Olson, E.R.2
  • 34
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley. M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Nikaido, H. 1996. Outer membrane, p. 29-47. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley. M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 29-47
    • Nikaido, H.1
  • 35
    • 0017687155 scopus 로고
    • Outer membrane of Salmonella, XIV. Reduced transmembrane diffusion rates in porin-deficient mutants
    • Nikaido, H., S. A. Song, L. Shaltiel, and M. Nurminen. 1977. Outer membrane of Salmonella, XIV. Reduced transmembrane diffusion rates in porin-deficient mutants. Biochem. Biophys. Res. Commun. 76:324-330.
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 324-330
    • Nikaido, H.1    Song, S.A.2    Shaltiel, L.3    Nurminen, M.4
  • 36
    • 0020522392 scopus 로고
    • Porin channels in Escherichia coli: Studies with β-lactams in intact cells
    • Nikaido, H., E. Y. Rosenberg, and J. Foulds. 1983. Porin channels in Escherichia coli: studies with β-lactams in intact cells. J. Bacteriol. 153:232-240.
    • (1983) J. Bacteriol. , vol.153 , pp. 232-240
    • Nikaido, H.1    Rosenberg, E.Y.2    Foulds, J.3
  • 37
    • 0027522569 scopus 로고
    • Influence of pH on bacterial gene expression
    • Olson, E. 1993. Influence of pH on bacterial gene expression. Mol. Microbiol. 8:5-14.
    • (1993) Mol. Microbiol. , vol.8 , pp. 5-14
    • Olson, E.1
  • 38
    • 0344094718 scopus 로고    scopus 로고
    • Personal communication
    • Olson, E. Personal communication.
    • Olson, E.1
  • 39
    • 0019970754 scopus 로고
    • Spectrophotometric assay for lysine decarboxylase
    • Phan, A. P. H., T. T. Ngo, and H. M. Lenhoff. 1982. Spectrophotometric assay for lysine decarboxylase. Anal. Biochem. 120:193-197.
    • (1982) Anal. Biochem. , vol.120 , pp. 193-197
    • Phan, A.P.H.1    Ngo, T.T.2    Lenhoff, H.M.3
  • 40
    • 0001427734 scopus 로고
    • Porin regulon of Escherichia coli
    • J. A. Hoch and T. J. Silhavy (ed.). ASM Press, Washington, D.C.
    • Pratt, L. A., and T. J. Silhavy. 1995. Porin regulon of Escherichia coli, p. 105-127. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction , pp. 105-127
    • Pratt, L.A.1    Silhavy, T.J.2
  • 41
    • 0030003230 scopus 로고    scopus 로고
    • Replacement of the sole histidynyl residue in OmpF porin from E. coli by threonine (H21T) does not affect channel structure and function
    • Saint, N., A. Prilipov, A. Hardmeyer, K.-L. Lou, T. Schirmer, and J. P. Rosenbusch. 1996. Replacement of the sole histidynyl residue in OmpF porin from E. coli by threonine (H21T) does not affect channel structure and function. Biochem. Biophys. Res. Commun. 223:118-122.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 118-122
    • Saint, N.1    Prilipov, A.2    Hardmeyer, A.3    Lou, K.-L.4    Schirmer, T.5    Rosenbusch, J.P.6
  • 42
    • 0000060960 scopus 로고    scopus 로고
    • pH-regulated genes and survival at extreme pH
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Slonczewski, J. L., and J. W. Foster. 1996. pH-regulated genes and survival at extreme pH, p. 1539-1549. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1539-1549
    • Slonczewski, J.L.1    Foster, J.W.2
  • 43
    • 0026542813 scopus 로고
    • Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH
    • Watson, N., D. S. Dunyak, E. L. Rosey, J. L. Slonczewski, and E. R. Olson. 1992. Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH. J. Bacteriol. 174:530-540.
    • (1992) J. Bacteriol. , vol.174 , pp. 530-540
    • Watson, N.1    Dunyak, D.S.2    Rosey, E.L.3    Slonczewski, J.L.4    Olson, E.R.5


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