메뉴 건너뛰기




Volumn 47, Issue 3, 2003, Pages 849-860

Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ACULEACIN A; AMIDASE; AMIDE; AMINO ACID; CEPHALOSPORIN; ELASTASE; FATTY ACID; HOMOSERINE; HYDROLASE; LACTONE; POLYPEPTIDE; PROTEIN AIID; PROTEIN DERIVATIVE; PYOCYANINE; UNCLASSIFIED DRUG;

EID: 0037238544     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03351.x     Document Type: Article
Times cited : (462)

References (58)
  • 1
    • 0035403603 scopus 로고    scopus 로고
    • Reaction of acylated homoserine lactone bacterial signaling molecules with oxidized halogen antimicrobials
    • Borchardt, S.A., Allain, E.J., Michels, J.J., Stearns, G.W., Kelly, R.F., and McCoy, W.F. (2001) Reaction of acylated homoserine lactone bacterial signaling molecules with oxidized halogen antimicrobials. Appl Environ Microbiol 67: 3174-3179.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3174-3179
    • Borchardt, S.A.1    Allain, E.J.2    Michels, J.J.3    Stearns, G.W.4    Kelly, R.F.5    McCoy, W.F.6
  • 3
    • 0033592926 scopus 로고    scopus 로고
    • Lethal paralysis ofCaenorhabditis elegans byPseudomo-nas aeruginosa
    • Darby, C., Cosma, C.L., Thomas, J.H., and Manoil, C. (1999) Lethal paralysis ofCaenorhabditis elegans byPseudomo-nas aeruginosa. Proc Natl Acad Sci USA 96: 15202-15207.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 15202-15207
    • Darby, C.1    Cosma, C.L.2    Thomas, J.H.3    Manoil, C.4
  • 5
    • 0034724191 scopus 로고    scopus 로고
    • AiiA, an enzymes that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora
    • Dong, Y.-H., Xu, J.-L., Li, X.-Z., and Zhang, L.-H. (2000) AiiA, an enzymes that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. Proc Natl Acad Sci USA 97: 3526-3531.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3526-3531
    • Dong, Y.-H.1    Xu, J.-L.2    Li, X.-Z.3    Zhang, L.-H.4
  • 6
    • 0035859128 scopus 로고    scopus 로고
    • Quenching quorum-sensing dependent bacterial infection by anN-acyl homoserine lactonase
    • Dong, Y.-H., Wang, L.-H., Xu, J.-L., Zhang, H.-B., Zhang, X.-F., and Zhang, L.-H. (2001) Quenching quorum-sensing dependent bacterial infection by anN-acyl homoserine lactonase.Nature 411: 813-817.
    • (2001) Nature , vol.411 , pp. 813-817
    • Dong, Y.-H.1    Wang, L.-H.2    Xu, J.-L.3    Zhang, H.-B.4    Zhang, X.-F.5    Zhang, L.-H.6
  • 7
    • 0036205598 scopus 로고    scopus 로고
    • Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species
    • Dong, Y.-H., Gusti, A.R., Zhang, Q., Xu, J.-L., and Zhang, L.-H. (2002) Identification of quorum-quenching N-acyl homoserine lactonases from Bacillus species. Appl Environ Microbiol 68: 1754-1759.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 1754-1759
    • Dong, Y.-H.1    Gusti, A.R.2    Zhang, Q.3    Xu, J.-L.4    Zhang, L.-H.5
  • 10
    • 0025117531 scopus 로고
    • Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: Interchangeability of the two anthranilate synthases and evolutionary implications
    • Essar, D.W., Eberly, L., Hadero, A., and Crawford, I. (1990) Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications. J Bacteriol 172: 884-900.
    • (1990) J Bacteriol , vol.172 , pp. 884-900
    • Essar, D.W.1    Eberly, L.2    Hadero, A.3    Crawford, I.4
  • 11
    • 0036137006 scopus 로고    scopus 로고
    • Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C
    • Fritz-Wolf, K., Koller, K.-P., Lange, G., Liesum, A., Sauber, K., Schreuder, H.,et al. (2002) Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C.Protein Sci 11: 92-103.
    • (2002) Protein Sci , vol.11 , pp. 92-103
    • Fritz-Wolf, K.1    Koller, K.-P.2    Lange, G.3    Liesum, A.4    Sauber, K.5    Schreuder, H.6
  • 12
    • 0029818809 scopus 로고    scopus 로고
    • Census and consensus in bacterial ecosystems: The LuxR-LuxI family of quorum-sensing transcriptional regulators
    • Fuqua, C., Winans, S.C., and Greenberg, E.P. (1996) Census and consensus in bacterial ecosystems: the LuxR-LuxI family of quorum-sensing transcriptional regulators. Annu Rev Microbiol 50:727-751.
    • (1996) Annu Rev Microbiol , vol.50 , pp. 727-751
    • Fuqua, C.1    Winans, S.C.2    Greenberg, E.P.3
  • 13
    • 0035685108 scopus 로고    scopus 로고
    • Pseudomonas aerug-inosa PAO1 kills Caenorhabditis elegans by cyanide poisoning
    • Gallagher, L.A., and Manoil, C. (2001) Pseudomonas aerug-inosa PAO1 kills Caenorhabditis elegans by cyanide poisoning. J Bacteriol 183: 6207-6214.
    • (2001) J Bacteriol , vol.183 , pp. 6207-6214
    • Gallagher, L.A.1    Manoil, C.2
  • 14
    • 0029854171 scopus 로고    scopus 로고
    • Eukaryotic interference with homoserine lactone mediated prokaryotic signaling
    • Givskov, M., de Nys, R., Manefield, M., Gram, L., Maximilien, R., Eberl, L., et al. (1996) Eukaryotic interference with homoserine lactone mediated prokaryotic signaling. J Bacteriol 178: 6618-6622.
    • (1996) J Bacteriol , vol.178 , pp. 6618-6622
    • Givskov, M.1    De Nys, R.2    Manefield, M.3    Gram, L.4    Maximilien, R.5    Eberl, L.6
  • 15
    • 0034730417 scopus 로고    scopus 로고
    • Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft
    • Hewitt, L., Kasche, V., Lummer, K., Lewis, R.J., Murshudov, G.N., Verma, C.S., et al. (2000) Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft. J Mol Biol 302: 887-898.
    • (2000) J Mol Biol , vol.302 , pp. 887-898
    • Hewitt, L.1    Kasche, V.2    Lummer, K.3    Lewis, R.J.4    Murshudov, G.N.5    Verma, C.S.6
  • 16
    • 0026669019 scopus 로고
    • Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression inStreptomyces lividans
    • Inokoshi, J., Takeshima, H., Ikeda, H., and Omura, S. (1992) Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression inStreptomyces lividans. Gene 119: 29-35.
    • (1992) Gene , vol.119 , pp. 29-35
    • Inokoshi, J.1    Takeshima, H.2    Ikeda, H.3    Omura, S.4
  • 17
    • 0030885191 scopus 로고    scopus 로고
    • Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases
    • Jakubowski, H. (1997) Aminoacyl thioester chemistry of class II aminoacyl-tRNA synthetases. Biochemistry 36: 11077-11085.
    • (1997) Biochemistry , vol.36 , pp. 11077-11085
    • Jakubowski, H.1
  • 18
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation
    • Jakubowski, H. (2000) Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J Biol Chem 275: 3957-3962.
    • (2000) J Biol Chem , vol.275 , pp. 3957-3962
    • Jakubowski, H.1
  • 19
    • 0033862847 scopus 로고    scopus 로고
    • Bacterial quorum-sensing in pathogenic relationships
    • de Kievit, T.R., and Iglewski, B.H. (2000) Bacterial quorum-sensing in pathogenic relationships. Infect Immun 68: 4839-4849.
    • (2000) Infect Immun , vol.68 , pp. 4839-4849
    • De Kievit, T.R.1    Iglewski, B.H.2
  • 20
    • 0010170654 scopus 로고    scopus 로고
    • Isolation of new Pseudomonas diminuta KAC-1 strain producing glu-taryl 7-aminocephalosporanic acid acylase
    • Kim, D.-W., Kang, S.-M., and Yoon, K.-H. (1999) Isolation of new Pseudomonas diminuta KAC-1 strain producing glu-taryl 7-aminocephalosporanic acid acylase. J Microbiol 37: 200-205.
    • (1999) J Microbiol , vol.37 , pp. 200-205
    • Kim, D.-W.1    Kang, S.-M.2    Yoon, K.-H.3
  • 21
    • 0035930509 scopus 로고    scopus 로고
    • Active site residues of cepha-losporin acylase are critical not only for enzymatic catalysis but also for post-translational modification
    • Kim, S., and Kim, Y. (2001) Active site residues of cepha-losporin acylase are critical not only for enzymatic catalysis but also for post-translational modification. J Biol Chem 276: 48376-48381.
    • (2001) J Biol Chem , vol.276 , pp. 48376-48381
    • Kim, S.1    Kim, Y.2
  • 22
    • 0034435442 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of cephalosporin acylase
    • Kim, Y., Yoon, K., Khang, Y., Turley, S., and Hol, W.G. (2000) The 2.0 Å crystal structure of cephalosporin acylase. Structure Fold Des 8: 1059-1068.
    • (2000) Structure Fold Des , vol.8 , pp. 1059-1068
    • Kim, Y.1    Yoon, K.2    Khang, Y.3    Turley, S.4    Hol, W.G.5
  • 23
    • 0033758742 scopus 로고    scopus 로고
    • Swarming of Pseudomonas aeruginosa is dependent on cell-cell signaling and requires flagella and pili
    • Köhler, T., Curty, L.K., Barja, F., van Delden, C., and Pechère, J.-C. (2000) Swarming of Pseudomonas aeruginosa is dependent on cell-cell signaling and requires flagella and pili. J Bacteriol 182: 5990-5996.
    • (2000) J Bacteriol , vol.182 , pp. 5990-5996
    • Köhler, T.1    Curty, L.K.2    Barja, F.3    Van Delden, C.4    Pechère, J.-C.5
  • 24
    • 0035859098 scopus 로고    scopus 로고
    • News and views: Plant microbiology - Quieting the raucous crowd
    • Leadbetter, J.R. (2001) News and views: plant microbiology - quieting the raucous crowd. Nature 411: 748-749.
    • (2001) Nature , vol.411 , pp. 748-749
    • Leadbetter, J.R.1
  • 25
    • 0034460299 scopus 로고    scopus 로고
    • Metabolism of acyl-homoserine lactone quorum-sensing signals by Vari-ovorax paradoxus
    • Leadbetter, J.R., and Greenberg, E.P. (2000) Metabolism of acyl-homoserine lactone quorum-sensing signals by Vari-ovorax paradoxus. J Bacteriol 182: 6921-6926.
    • (2000) J Bacteriol , vol.182 , pp. 6921-6926
    • Leadbetter, J.R.1    Greenberg, E.P.2
  • 26
    • 0036328528 scopus 로고    scopus 로고
    • Genes encoding theN-Acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis
    • Lee, S.J., Park, S.Y., Lee, J.J., Yum, D.Y., Koo, B.T., and Lee, J.K. (2002) Genes encoding theN-Acyl homoserine lactone-degrading enzyme are widespread in many subspecies of Bacillus thuringiensis. Appl Environ Microbiol 68: 3919-3924.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3919-3924
    • Lee, S.J.1    Park, S.Y.2    Lee, J.J.3    Yum, D.Y.4    Koo, B.T.5    Lee, J.K.6
  • 27
    • 0034671855 scopus 로고    scopus 로고
    • The role ofa-amino group of the N-terminal serine of b-subunit for enzyme catalysis and autoproteolytic activation of glutaryl 7-aminocephalosporanic acid acylase
    • Lee, Y.S., Kim, H.W., and Park, S.S. (2000) The role ofa-amino group of the N-terminal serine of b-subunit for enzyme catalysis and autoproteolytic activation of glutaryl 7-aminocephalosporanic acid acylase. J Biol Chem 275: 39200-39206.
    • (2000) J Biol Chem , vol.275 , pp. 39200-39206
    • Lee, Y.S.1    Kim, H.W.2    Park, S.S.3
  • 28
    • 0033564384 scopus 로고    scopus 로고
    • In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130
    • Li, Y., Chen, J., Jiang, W., Mao, X., Zhao, G., and Wang, E. (1999) In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130. Eur J Biochem 262: 713-719.
    • (1999) Eur J Biochem , vol.262 , pp. 713-719
    • Li, Y.1    Chen, J.2    Jiang, W.3    Mao, X.4    Zhao, G.5    Wang, E.6
  • 29
    • 0031467411 scopus 로고    scopus 로고
    • Quorum-sensing and Chro-mobacterium violaceum: Exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones
    • McClean, K.H., Winson, M.K., Fish, L., Taylor, A., Chhabra, S.R., Camara, M.,et al. (1997) Quorum-sensing and Chro-mobacterium violaceum: exploitation of violacein production and inhibition for the detection of N-acylhomoserine lactones. Microbiology 143: 3703-3711.
    • (1997) Microbiology , vol.143 , pp. 3703-3711
    • McClean, K.H.1    Winson, M.K.2    Fish, L.3    Taylor, A.4    Chhabra, S.R.5    Camara, M.6
  • 30
    • 0035850792 scopus 로고    scopus 로고
    • Crystal structures of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism
    • McVey, C.E., Walsh, M.A., Dodson, G.G., Wilson, K.S., and Brannigan, J.A. (2001) Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism. J Mol Biol 313: 139-150.
    • (2001) J Mol Biol , vol.313 , pp. 139-150
    • McVey, C.E.1    Walsh, M.A.2    Dodson, G.G.3    Wilson, K.S.4    Brannigan, J.A.5
  • 31
    • 0033060727 scopus 로고    scopus 로고
    • Evidence that halogenated furanones from Delisea pulchra inhibit acylated homoserine lactone (AHL)-mediated gene expression by displacing the AHL signal from its receptor protein
    • Manefield, M., de Nys, R., Kumar, N., Read, R., Givskov, M., Steinberg, P., and Kjelleberg, S. (1999) Evidence that halogenated furanones from Delisea pulchra inhibit acylated homoserine lactone (AHL)-mediated gene expression by displacing the AHL signal from its receptor protein. Microbiology 145: 283-291.
    • (1999) Microbiology , vol.145 , pp. 283-291
    • Manefield, M.1    De Nys, R.2    Kumar, N.3    Read, R.4    Givskov, M.5    Steinberg, P.6    Kjelleberg, S.7
  • 33
    • 0021972478 scopus 로고
    • Molecular cloning and structure of the gene for 7-b-(4-carboxybutanamido) cephalosporanic acid acylase from a Pseudomonas strain
    • Matsuda, A., and Komatsu, K. (1985) Molecular cloning and structure of the gene for 7-b-(4-carboxybutanamido) cephalosporanic acid acylase from a Pseudomonas strain. J Bacteriol 163: 1222-1228.
    • (1985) J Bacteriol , vol.163 , pp. 1222-1228
    • Matsuda, A.1    Komatsu, K.2
  • 34
    • 0023544883 scopus 로고
    • Nucleotide sequence of the genes for two distinct cephalosporin acylases from a Pseudomonas strain
    • Matsuda, A., Toma, K., and Komatsu, K. (1987) Nucleotide sequence of the genes for two distinct cephalosporin acylases from a Pseudomonas strain. J Bacteriol 169: 5821-5826.
    • (1987) J Bacteriol , vol.169 , pp. 5821-5826
    • Matsuda, A.1    Toma, K.2    Komatsu, K.3
  • 35
    • 0036016826 scopus 로고    scopus 로고
    • The autoregulatory role of EsaR, a quorum-sensing regulator in Pantoea stewartii ssp. stewartii: Evidence for a repressor function
    • Minogue, T.D., Trebra, M.W., Bernhard, F., and Bodman,S.B. (2002) The autoregulatory role of EsaR, a quorum-sensing regulator in Pantoea stewartii ssp. stewartii: evidence for a repressor function. Mol Microbiol 44: 1625-1635.
    • (2002) Mol Microbiol , vol.44 , pp. 1625-1635
    • Minogue, T.D.1    Trebra, M.W.2    Bernhard, F.3    Bodman, S.B.4
  • 36
    • 0023481348 scopus 로고
    • Complete nucleotide sequence of the penicillin G acylase gene and the flanking regions, and its expression in Escherichia coli
    • Oh, S.J., Kim, Y.C., Park, Y.W., Min, S.Y., Kim, I.S., and Kang, H.S. (1987) Complete nucleotide sequence of the penicillin G acylase gene and the flanking regions, and its expression in Escherichia coli. Gene 56: 87-97.
    • (1987) Gene , vol.56 , pp. 87-97
    • Oh, S.J.1    Kim, Y.C.2    Park, Y.W.3    Min, S.Y.4    Kim, I.S.5    Kang, H.S.6
  • 37
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen, C., and Rouvinen, J. (2000) Structural comparison of Ntn-hydrolases. Protein Sci 9: 2329-2337.
    • (2000) Protein Sci , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 39
    • 0030930248 scopus 로고    scopus 로고
    • Role of Pseudomonas aeruginosa las and rhl quorum-sensing systems in the control of elastase and rhamnolipid biosynthesis genes
    • Pearson, J.P., Pesci, E.C., and Iglewski, B.H. (1997) Role of Pseudomonas aeruginosa las and rhl quorum-sensing systems in the control of elastase and rhamnolipid biosynthesis genes. J Bacteriol 179: 5756-5767.
    • (1997) J Bacteriol , vol.179 , pp. 5756-5767
    • Pearson, J.P.1    Pesci, E.C.2    Iglewski, B.H.3
  • 40
    • 0027412028 scopus 로고
    • Conjugation factor ofAgrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction
    • Piper, K.R., Beck von Bodman, S., and Farrand, S.K. (1993) Conjugation factor ofAgrobacterium tumefaciens regulates Ti plasmid transfer by autoinduction. Nature 362: 448-450.
    • (1993) Nature , vol.362 , pp. 448-450
    • Piper, K.R.1    Beck von Bodman, S.2    Farrand, S.K.3
  • 41
    • 0034712760 scopus 로고    scopus 로고
    • Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa
    • Rashid, M.H., and Kornberg, A. (2000) Inorganic polyphosphate is needed for swimming, swarming, and twitching motilities of Pseudomonas aeruginosa. Proc Natl Acad Sci USA 97: 4885-4890.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4885-4890
    • Rashid, M.H.1    Kornberg, A.2
  • 42
    • 0034517622 scopus 로고    scopus 로고
    • How Delisea pulchra furanones affect quorum sensing and swarming motility in Serratia liquefaciens MG1
    • Rasmussen, T.B., Manefield, M., Andersen, J.B., Eberl, L., Anthoni, U., Christophersen, C.,et al. (2000) How Delisea pulchra furanones affect quorum sensing and swarming motility in Serratia liquefaciens MG1. Microbiology 146:3237-3244.
    • (2000) Microbiology , vol.146 , pp. 3237-3244
    • Rasmussen, T.B.1    Manefield, M.2    Andersen, J.B.3    Eberl, L.4    Anthoni, U.5    Christophersen, C.6
  • 43
    • 0036224501 scopus 로고    scopus 로고
    • Genetically programmed autoinducer destruction reduces virulence gene expression and swarming motility in Pseudomonas aeruginosa PAO1
    • Reimmann, C., Ginet, N., Michel, L., Keel, C., Michaux, P., Krishnapillai, V., et al. (2002) Genetically programmed autoinducer destruction reduces virulence gene expression and swarming motility in Pseudomonas aeruginosa PAO1. Microbiology 148: 923-932.
    • (2002) Microbiology , vol.148 , pp. 923-932
    • Reimmann, C.1    Ginet, N.2    Michel, L.3    Keel, C.4    Michaux, P.5    Krishnapillai, V.6
  • 45
    • 0023056887 scopus 로고
    • Penicillin acylase from E. coli: Unique gene-protein relation
    • Schumacher, G., Sizmann, D., Haug, H., Buckel, P., and Bock, A. (1986) Penicillin acylase from E. coli: unique gene-protein relation. Nucleic Acids Res 14: 5713-5727.
    • (1986) Nucleic Acids Res , vol.14 , pp. 5713-5727
    • Schumacher, G.1    Sizmann, D.2    Haug, H.3    Buckel, P.4    Bock, A.5
  • 46
    • 0026011339 scopus 로고
    • Escherichia-Pseudomonas shuttle vectors derived from pUC18/19
    • Schweizer, H.P. (1991) Escherichia-Pseudomonas shuttle vectors derived from pUC18/19. Gene 97: 109-121.
    • (1991) Gene , vol.97 , pp. 109-121
    • Schweizer, H.P.1
  • 47
    • 0023506006 scopus 로고
    • Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea
    • Staskawicz, B., Dahlbeck, D., Keen, N., and Napoli, C. (1987) Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea. J Bacteriol 169: 5789-5794.
    • (1987) J Bacteriol , vol.169 , pp. 5789-5794
    • Staskawicz, B.1    Dahlbeck, D.2    Keen, N.3    Napoli, C.4
  • 48
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen
    • Stover, C.K., Pham, X.Q., Erwin, A.L., Mizoguchi, S.D., Warrener, P., Hickey, M.J., et al. (2000) Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. Nature 406: 959-964.
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1    Pham, X.Q.2    Erwin, A.L.3    Mizoguchi, S.D.4    Warrener, P.5    Hickey, M.J.6
  • 49
    • 0000182225 scopus 로고
    • Methods
    • Wood, W.B. (ed.). Cold Spring Harbour, NY: Cold Spring Harbour Laboratory Press
    • Sulston, J., and Hodgkin, J. (1988) Methods. In The Nematode Caenorhabditis elegans. Wood, W.B. (ed.). Cold Spring Harbour, NY: Cold Spring Harbour Laboratory Press, pp. 587-606.
    • (1988) The Nematode Caenorhabditis Elegans , pp. 587-606
    • Sulston, J.1    Hodgkin, J.2
  • 50
    • 0024573701 scopus 로고
    • A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: Purification and characterization
    • Takeshima, H., Inokoshi, J., Takada, Y., Tanaka, H., and Omura, S. (1989) A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J Biochem 105: 606-610.
    • (1989) J Biochem , vol.105 , pp. 606-610
    • Takeshima, H.1    Inokoshi, J.2    Takada, Y.3    Tanaka, H.4    Omura, S.5
  • 51
    • 0030045365 scopus 로고    scopus 로고
    • Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection
    • Tang, H.B., DiMango, E., Bryan, R., Gambello, M., Iglewski, B.H., Goldberg, J.B., and Prince, A. (1996) Contribution of specific Pseudomonas aeruginosa virulence factors to pathogenesis of pneumonia in a neonatal mouse model of infection. Infect Immun 64: 37-43.
    • (1996) Infect Immun , vol.64 , pp. 37-43
    • Tang, H.B.1    DiMango, E.2    Bryan, R.3    Gambello, M.4    Iglewski, B.H.5    Goldberg, J.B.6    Prince, A.7
  • 52
    • 0034034838 scopus 로고    scopus 로고
    • Plants secrete substances that mimic bacterial N-acyl homoserine lactone signal activities and affect population density-dependent behaviors in associated bacteria
    • Teplitski, M., Robinson, J.B., and Bauer, W.D. (2000) Plants secrete substances that mimic bacterial N-acyl homoserine lactone signal activities and affect population density-dependent behaviors in associated bacteria. Mol Plant-Microbe Interact 13: 637-648.
    • (2000) Mol Plant-Microbe Interact , vol.13 , pp. 637-648
    • Teplitski, M.1    Robinson, J.B.2    Bauer, W.D.3
  • 54
    • 0033006992 scopus 로고    scopus 로고
    • The novel transmembrane Escherichia coli proteins involved in the amino acid efflux
    • Zakataeva, N.P., Aleshin, V.V., Tokmakova, I.L., Troshin, P.V., and Livshits, V.A. (1999) The novel transmembrane Escherichia coli proteins involved in the amino acid efflux. FEBS Lett 452: 228-232.
    • (1999) FEBS Lett , vol.452 , pp. 228-232
    • Zakataeva, N.P.1    Aleshin, V.V.2    Tokmakova, I.L.3    Troshin, P.V.4    Livshits, V.A.5
  • 55
    • 0037007116 scopus 로고    scopus 로고
    • Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens
    • Zhang, H.-B., Wang, L.-H., and Zhang, L.-H. (2002) Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens. Proc Natl Acad Sci USA 99: 4638-4643.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4638-4643
    • Zhang, H.-B.1    Wang, L.-H.2    Zhang, L.-H.3
  • 56
    • 0027479479 scopus 로고
    • Agrobacterium conjugation and gene regulation by N-acyl-L-homoserine lactones
    • Zhang, L.-H., Murphy, P.J., Kerr, A., and Tate, M.E. (1993) Agrobacterium conjugation and gene regulation by N-acyl-L-homoserine lactones. Nature 362: 446-447.
    • (1993) Nature , vol.362 , pp. 446-447
    • Zhang, L.-H.1    Murphy, P.J.2    Kerr, A.3    Tate, M.E.4
  • 57
    • 0031888391 scopus 로고    scopus 로고
    • High affinity binding of albicidin phytotoxins by the AlbA protein from Klebsiella oxytoca
    • Zhang, L.-H., Xu, J., and Birch, R.G. (1998) High affinity binding of albicidin phytotoxins by the AlbA protein from Klebsiella oxytoca. Microbiology 144: 555-559.
    • (1998) Microbiology , vol.144 , pp. 555-559
    • Zhang, L.-H.1    Xu, J.2    Birch, R.G.3
  • 58
    • 0031690671 scopus 로고    scopus 로고
    • Analogs of the autoinducer 3-oxooctanoyl-homoserine lactone strongly inhibit activity of the TraR protein of Agrobacterium tumefaciens
    • Zhu, J., Beaber, J.W., More, M.I., Fuqua, C., Eberhard, A., and Winans, S.C. (1998) Analogs of the autoinducer 3-oxooctanoyl-homoserine lactone strongly inhibit activity of the TraR protein of Agrobacterium tumefaciens. J Bacteriol 180: 5398-5405.
    • (1998) J Bacteriol , vol.180 , pp. 5398-5405
    • Zhu, J.1    Beaber, J.W.2    More, M.I.3    Fuqua, C.4    Eberhard, A.5    Winans, S.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.