메뉴 건너뛰기




Volumn 72, Issue 3, 2006, Pages 1910-1924

Conservation of the Pho regulon in Pseudomonas fluorescens Pf0-1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ENZYMES; ESCHERICHIA COLI; GENES; IRON; MOLECULES; PHOSPHATES;

EID: 33644962079     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.3.1910-1924.2006     Document Type: Article
Times cited : (102)

References (65)
  • 1
    • 3342921823 scopus 로고    scopus 로고
    • Characterization and genetic manipulation of peptide synthetases in Pseudomonas aeruginosa PAO1 in order to generate novel pyoverdines
    • Ackerley, D. F., and I. L. Lamont. 2004. Characterization and genetic manipulation of peptide synthetases in Pseudomonas aeruginosa PAO1 in order to generate novel pyoverdines. Chem. Biol. 11:971-980.
    • (2004) Chem. Biol. , vol.11 , pp. 971-980
    • Ackerley, D.F.1    Lamont, I.L.2
  • 3
    • 0025324993 scopus 로고
    • Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the regulatory gene for the phosphate regulon
    • Anba, J., M. Bidaud, M. L. Vasil, and A. Lazdunski. 1990. Nucleotide sequence of the Pseudomonas aeruginosa phoB gene, the regulatory gene for the phosphate regulon. J. Bacteriol. 172:4685-4689.
    • (1990) J. Bacteriol. , vol.172 , pp. 4685-4689
    • Anba, J.1    Bidaud, M.2    Vasil, M.L.3    Lazdunski, A.4
  • 4
    • 0031941653 scopus 로고
    • Regulation of phosphate assimilation in Rhizobium (Sinorhizobium) meliloti
    • Bardin, S. D., and T. M. Finan. 1689. Regulation of phosphate assimilation in Rhizobium (Sinorhizobium) meliloti. Genetics 148:1689-1700.
    • (1689) Genetics , vol.148 , pp. 1689-1700
    • Bardin, S.D.1    Finan, T.M.2
  • 5
    • 0347325071 scopus 로고    scopus 로고
    • Lysogeny at mid-twentieth century: P1, P2, and other experimental systems
    • Bertani, G. 2004. Lysogeny at mid-twentieth century: P1, P2, and other experimental systems. J. Bacteriol. 186:595-600.
    • (2004) J. Bacteriol. , vol.186 , pp. 595-600
    • Bertani, G.1
  • 6
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman, J. E. 1992. Structure and mechanism of alkaline phosphatase. Annu. Rev. Biophys. Biomol. Struct. 21:441-483.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 7
    • 0025195680 scopus 로고
    • Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria
    • de Lorenzo, V., M. Herrero, U. Jakubzik, and K. N. Timmis. 1990. Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria. J. Bacteriol. 172:6568-6572.
    • (1990) J. Bacteriol. , vol.172 , pp. 6568-6572
    • De Lorenzo, V.1    Herrero, M.2    Jakubzik, U.3    Timmis, K.N.4
  • 8
    • 0029849654 scopus 로고    scopus 로고
    • A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD
    • Eder, S., L. Shi, K. Jensen, K. Yamane, and F. M. Hulett. 1996. A Bacillus subtilis secreted phosphodiesterase/alkaline phosphatase is the product of a Pho regulon gene, phoD. Microbiology 142:2041-2047.
    • (1996) Microbiology , vol.142 , pp. 2041-2047
    • Eder, S.1    Shi, L.2    Jensen, K.3    Yamane, K.4    Hulett, F.M.5
  • 9
    • 0345263516 scopus 로고
    • An apaH mutation causes AppppA to accumulate and affects motility and catabolite repression in Escherichia coli
    • Farr, S. B., D. N. Arnosti, M. J. Chamberlin, and B. N. Ames. 1989. An apaH mutation causes AppppA to accumulate and affects motility and catabolite repression in Escherichia coli. Proc. Natl. Acad. Sci. USA 86:5010-5014.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5010-5014
    • Farr, S.B.1    Arnosti, D.N.2    Chamberlin, M.J.3    Ames, B.N.4
  • 10
    • 0018162940 scopus 로고
    • Isolation of Escherichia coli mutants with changed regulation of uracil uptake
    • Fast, R. 1978. Isolation of Escherichia coli mutants with changed regulation of uracil uptake. J. Bacteriol. 136:839-843.
    • (1978) J. Bacteriol. , vol.136 , pp. 839-843
    • Fast, R.1
  • 11
    • 0023924421 scopus 로고
    • Phosphate regulation in Pseudomonas aeruginosa: Cloning of the alkaline phosphatase gene and identification of phoB- and phoR-like genes
    • Filloux, A., M. Bally, C. Soscia, M. Murgier, and A. Lazdunski. 1988. Phosphate regulation in Pseudomonas aeruginosa: cloning of the alkaline phosphatase gene and identification of phoB- and phoR-like genes. Mol. Gen. Genet. 212:510-513.
    • (1988) Mol. Gen. Genet. , vol.212 , pp. 510-513
    • Filloux, A.1    Bally, M.2    Soscia, C.3    Murgier, M.4    Lazdunski, A.5
  • 12
    • 0027229166 scopus 로고
    • AppppA-binding protein E89 is the Escherichia coli heat shock protein ClpB
    • Fuge, E. K., and S. B. Farr. 1993. AppppA-binding protein E89 is the Escherichia coli heat shock protein ClpB. J. Bacteriol. 175:2321-2326.
    • (1993) J. Bacteriol. , vol.175 , pp. 2321-2326
    • Fuge, E.K.1    Farr, S.B.2
  • 13
    • 0033566587 scopus 로고    scopus 로고
    • Fluorogenic substrates based on fluorinated umbelliferones for continuous assays of phosphatases and beta-galactosidases
    • Gee, K. R., W. C. Sun, M. K. Bhalgat, R. H. Upson, D. H. Klaubert, K. A. Latham, and R. P. Haugland. 1999. Fluorogenic substrates based on fluorinated umbelliferones for continuous assays of phosphatases and beta-galactosidases. Anal. Biochem. 273:41-48.
    • (1999) Anal. Biochem. , vol.273 , pp. 41-48
    • Gee, K.R.1    Sun, W.C.2    Bhalgat, M.K.3    Upson, R.H.4    Klaubert, D.H.5    Latham, K.A.6    Haugland, R.P.7
  • 14
    • 0033988998 scopus 로고    scopus 로고
    • Regulation of stalk elongation by phosphate in Caulobacter crescentus
    • Gonin, M., E. M. Quardokus, D. O'Donnol, J. Maddock, and Y. V. Brun. 2000. Regulation of stalk elongation by phosphate in Caulobacter crescentus. J. Bacteriol. 182:337-347.
    • (2000) J. Bacteriol. , vol.182 , pp. 337-347
    • Gonin, M.1    Quardokus, E.M.2    O'Donnol, D.3    Maddock, J.4    Brun, Y.V.5
  • 15
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 16
    • 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 aeruginosa 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 aeruginosa 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
  • 17
    • 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
  • 18
    • 0032760684 scopus 로고    scopus 로고
    • The mechanism of the alkaline phosphatase reaction: Insights from NMR, crystallography and site-specific mutagenesis
    • Holtz, K. M., and E. R. Kantrowitz. 1999. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis. FEBS Lett. 462:7-11.
    • (1999) FEBS Lett. , vol.462 , pp. 7-11
    • Holtz, K.M.1    Kantrowitz, E.R.2
  • 19
    • 0029976302 scopus 로고    scopus 로고
    • The signal-transduction network for Pho regulation in Bacillus subtilis
    • Hulett, F. M. 1996. The signal-transduction network for Pho regulation in Bacillus subtilis. Mol. Microbiol. 19:933-939.
    • (1996) Mol. Microbiol. , vol.19 , pp. 933-939
    • Hulett, F.M.1
  • 20
    • 0038659577 scopus 로고    scopus 로고
    • Optimization and validation of a rapid method to determine citrate and inorganic phosphate in milk by capillary electrophoresis
    • Izco, J. M., M. Tormo, A. Harris, P. S. Tong, and R. Jimenez-Flores. 2003. Optimization and validation of a rapid method to determine citrate and inorganic phosphate in milk by capillary electrophoresis. J. Dairy Sci. 86:86-95.
    • (2003) J. Dairy Sci. , vol.86 , pp. 86-95
    • Izco, J.M.1    Tormo, M.2    Harris, A.3    Tong, P.S.4    Jimenez-Flores, R.5
  • 22
    • 0036063913 scopus 로고    scopus 로고
    • The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway
    • Kim, A. D., A. S. Baker, D. Dunaway-Mariano, W. W. Metcalf, B. L. Wanner, and B. M. Martin. 2002. The 2-aminoethylphosphonate-specific transaminase of the 2-aminoethylphosphonate degradation pathway. J. Bacteriol. 184:4134-4140.
    • (2002) J. Bacteriol. , vol.184 , pp. 4134-4140
    • Kim, A.D.1    Baker, A.S.2    Dunaway-Mariano, D.3    Metcalf, W.W.4    Wanner, B.L.5    Martin, B.M.6
  • 23
    • 43349086724 scopus 로고
    • Two simple media for the demonstration of pyocyanin and fluorescein
    • King, E. O., M. K. Ward, and D. E. Raney. 1954. Two simple media for the demonstration of pyocyanin and fluorescein. J. Lab. Clin. Med. 44:301-307.
    • (1954) J. Lab. Clin. Med. , vol.44 , pp. 301-307
    • King, E.O.1    Ward, M.K.2    Raney, D.E.3
  • 24
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., P. H. Elzer, D. S. Hill, G. T. Robertson, M. A. Farris, R. M. Roop II, and K. M. Peterson. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop II, R.M.6    Peterson, K.M.7
  • 25
    • 4544275338 scopus 로고    scopus 로고
    • Global transcriptional analysis of the phosphate starvation response in Sinorhizobium meliloti strains 1021 and 2011
    • Krol, E., and A. Becker. 2004. Global transcriptional analysis of the phosphate starvation response in Sinorhizobium meliloti strains 1021 and 2011. Mol. Genet. Genom. 272:1-17.
    • (2004) Mol. Genet. Genom. , vol.272 , pp. 1-17
    • Krol, E.1    Becker, A.2
  • 26
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeuroginosa fimbrial cup genes
    • Kulasekara, H. D., I. Ventre, B. R. Kulasekara, A. Lazdunski, A. Filloux, and S. Lory. 2005. A novel two-component system controls the expression of Pseudomonas aeuroginosa fimbrial cup genes. Mol. Microbiol. 55:368-380.
    • (2005) Mol. Microbiol. , vol.55 , pp. 368-380
    • Kulasekara, H.D.1    Ventre, I.2    Kulasekara, B.R.3    Lazdunski, A.4    Filloux, A.5    Lory, S.6
  • 27
    • 3042786311 scopus 로고    scopus 로고
    • Mini-Tn7 transposons for site-specific tagging of bacteria with fluorescent proteins
    • Lambertsen, L., C. Sternberg, and S. Molin. 2004. Mini-Tn7 transposons for site-specific tagging of bacteria with fluorescent proteins. Environ. Microbiol. 6:726-732.
    • (2004) Environ. Microbiol. , vol.6 , pp. 726-732
    • Lambertsen, L.1    Sternberg, C.2    Molin, S.3
  • 28
    • 12344263847 scopus 로고    scopus 로고
    • Identification of the gene for the monomeric alkaline phosphatase of Vibrio cholerae serogroup O1 strain
    • Majumdar, A., A. Ghatak, and R. K. Ghosh. 2005. Identification of the gene for the monomeric alkaline phosphatase of Vibrio cholerae serogroup O1 strain. Gene 344:251-258.
    • (2005) Gene , vol.344 , pp. 251-258
    • Majumdar, A.1    Ghatak, A.2    Ghosh, R.K.3
  • 29
    • 0024299476 scopus 로고
    • Flagellar dynamometer controls swarmer cell differentiation of Vibrio parahaemolyticus
    • McCarter, L., M. Hilmen, and M. Silverman. 1988. Flagellar dynamometer controls swarmer cell differentiation of Vibrio parahaemolyticus. Cell 54:345-351.
    • (1988) Cell , vol.54 , pp. 345-351
    • McCarter, L.1    Hilmen, M.2    Silverman, M.3
  • 31
    • 0034758946 scopus 로고    scopus 로고
    • Expression of the Pho regulon negatively regulates biofilm formation by Pseudomonas aureofaciens PA147-2
    • Monds, R. D., M. W. Silby, and H. K. Mahanty. 2001. Expression of the Pho regulon negatively regulates biofilm formation by Pseudomonas aureofaciens PA147-2. Mol. Microbiol. 42:415-426.
    • (2001) Mol. Microbiol. , vol.42 , pp. 415-426
    • Monds, R.D.1    Silby, M.W.2    Mahanty, H.K.3
  • 33
    • 14644395585 scopus 로고    scopus 로고
    • Twin-arginine-specific protein export in Escherichia coli
    • Muller, M. 2005. Twin-arginine-specific protein export in Escherichia coli. Res. Microbiol. 156:131-136.
    • (2005) Res. Microbiol. , vol.156 , pp. 131-136
    • Muller, M.1
  • 35
    • 0029947312 scopus 로고    scopus 로고
    • Molecular analysis of the phosphate-specific transport (pst) operon of Pseudomonas aeruginosa
    • Nikata, T., Y. Sakai, K. Shibat, J. Kato, A. Kuroda, and H. Ohtake. 1996. Molecular analysis of the phosphate-specific transport (pst) operon of Pseudomonas aeruginosa. Mol. Gen. Genet. 250:692-698.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 692-698
    • Nikata, T.1    Sakai, Y.2    Shibat, K.3    Kato, J.4    Kuroda, A.5    Ohtake, H.6
  • 36
    • 0033026468 scopus 로고    scopus 로고
    • Identification of a Streptococcus pneumoniae gene locus encoding proteins of an ABC phosphate transporter and a two-component regulatory system
    • Novak, R., A. Cauwels, E. Charpentier, and E. Tuomanen. 1999. Identification of a Streptococcus pneumoniae gene locus encoding proteins of an ABC phosphate transporter and a two-component regulatory system. J. Bacteriol. 181:1126-1133.
    • (1999) J. Bacteriol. , vol.181 , pp. 1126-1133
    • Novak, R.1    Cauwels, A.2    Charpentier, E.3    Tuomanen, E.4
  • 37
    • 0037062507 scopus 로고    scopus 로고
    • Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis
    • Ochsner, U. A., A. Snyder, A. I. Vasil, and M. L. Vasil. 2002. Effects of the twin-arginine translocase on secretion of virulence factors, stress response, and pathogenesis. Proc. Natl. Acad. Sci. USA 99:8312-8317.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8312-8317
    • Ochsner, U.A.1    Snyder, A.2    Vasil, A.I.3    Vasil, M.L.4
  • 38
    • 2342470541 scopus 로고    scopus 로고
    • Plant purple acid phosphatases-genes, structures and biological function
    • Olczak, M., B. Morawiecka, and W. Watorek. 2003. Plant purple acid phosphatases-genes, structures and biological function. Acta Biochim. Pol. 50:1245-1256.
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 1245-1256
    • Olczak, M.1    Morawiecka, B.2    Watorek, W.3
  • 40
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • Palmer, T., F. Sargent, and B. C. Berks. 2005. Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends Microbiol. 13:175-180.
    • (2005) Trends Microbiol. , vol.13 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 41
    • 0026460088 scopus 로고
    • Stimulation of glucose catabolism in Escherichia coli by a potential futile cycle
    • Patnaik, R., W. D. Roof, R. F. Young, and J. C. Liao. 1992. Stimulation of glucose catabolism in Escherichia coli by a potential futile cycle. J. Bacteriol. 174:7527-7532.
    • (1992) J. Bacteriol. , vol.174 , pp. 7527-7532
    • Patnaik, R.1    Roof, W.D.2    Young, R.F.3    Liao, J.C.4
  • 42
    • 0025079661 scopus 로고
    • Molecular aspects of phosphate transport in Escherichia coli
    • Rao, N. N., and A. Torriani. 1990. Molecular aspects of phosphate transport in Escherichia coli. Mol. Microbiol. 4:1083-1090.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1083-1090
    • Rao, N.N.1    Torriani, A.2
  • 43
    • 0024730183 scopus 로고
    • Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12
    • Roa, B. B., D. M. Connolly, and M. E. Winkler. 1989. Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12. J. Bacteriol. 171:4767-4777.
    • (1989) J. Bacteriol. , vol.171 , pp. 4767-4777
    • Roa, B.B.1    Connolly, D.M.2    Winkler, M.E.3
  • 45
    • 0027134384 scopus 로고
    • Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis
    • Schweizer, H. P. 1993. Small broad-host-range gentamycin resistance gene cassettes for site-specific insertion and deletion mutagenesis. BioTechniques 15:831-833.
    • (1993) BioTechniques , vol.15 , pp. 831-833
    • Schweizer, H.P.1
  • 46
    • 0030922378 scopus 로고    scopus 로고
    • Structure and gene-polypeptide relationships of the region encoding glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of Pseudomonas aeruginosa
    • Schweizer, H. P., R. Jump, and C. Po. 1997. Structure and gene-polypeptide relationships of the region encoding glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of Pseudomonas aeruginosa. Microbiology 143:1287-1297.
    • (1997) Microbiology , vol.143 , pp. 1287-1297
    • Schweizer, H.P.1    Jump, R.2    Po, C.3
  • 47
    • 0024004229 scopus 로고
    • Regulation of components of the Pseudomonas aeruginosa phosphate-starvation-inducible regulon in Escherichia coli
    • Siehnel, R. J., E. A. Worobec, and R. E. Hancock. 1988. Regulation of components of the Pseudomonas aeruginosa phosphate-starvation-inducible regulon in Escherichia coli. Mol. Microbiol. 2:347-352.
    • (1988) Mol. Microbiol. , vol.2 , pp. 347-352
    • Siehnel, R.J.1    Worobec, E.A.2    Hancock, R.E.3
  • 48
    • 6044274610 scopus 로고    scopus 로고
    • Use of in vivo expression technology to identify genes important in growth and survival of Pseudomonas fluorescens Pf0-1 in soil: Discovery of expressed sequences with novel genetic organization
    • Silby, M. W., and S. B. Levy. 2004. Use of in vivo expression technology to identify genes important in growth and survival of Pseudomonas fluorescens Pf0-1 in soil: discovery of expressed sequences with novel genetic organization. J. Bacteriol. 186:7411-7419.
    • (2004) J. Bacteriol. , vol.186 , pp. 7411-7419
    • Silby, M.W.1    Levy, S.B.2
  • 49
    • 0021027842 scopus 로고
    • A broad host range system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 50
    • 0037244560 scopus 로고    scopus 로고
    • Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and -independent pathways
    • Slater, H., M. Crow, L. Everson, and G. P. Salmond. 2003. Phosphate availability regulates biosynthesis of two antibiotics, prodigiosin and carbapenem, in Serratia via both quorum-sensing-dependent and -independent pathways. Mol. Microbiol. 47:303-320.
    • (2003) Mol. Microbiol. , vol.47 , pp. 303-320
    • Slater, H.1    Crow, M.2    Everson, L.3    Salmond, G.P.4
  • 51
    • 0033764648 scopus 로고    scopus 로고
    • The causes of Pseudomonas diversity
    • Spiers, A. J., A. Buckling, and P. B. Rainey. 2000. The causes of Pseudomonas diversity. Microbiology 146:2345-2350.
    • (2000) Microbiology , vol.146 , pp. 2345-2350
    • Spiers, A.J.1    Buckling, A.2    Rainey, P.B.3
  • 52
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley, N. R., T. Palmer, and B. C. Berks. 2000. The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275:11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 53
    • 0032213669 scopus 로고
    • Expression and regulation of phosphate stress inducible genes in Sinorhizobium meliloti
    • Summers, M. L., J. G. Elkins, B. A. Elliott, and T. R. McDermott. 1994. Expression and regulation of phosphate stress inducible genes in Sinorhizobium meliloti. Mol. Plant-Microbe Interact. 11:1094-1101.
    • (1994) Mol. Plant-Microbe Interact. , vol.11 , pp. 1094-1101
    • Summers, M.L.1    Elkins, J.G.2    Elliott, B.A.3    McDermott, T.R.4
  • 54
    • 0034982194 scopus 로고    scopus 로고
    • Molecular analysis of Mycobacterium tuberculosis phosphate specific transport system in Mycobacterium smegmatis. Characterization of recombinant 38 kDa (PstS-1)
    • Torres, A., M. D. Juarez, R. Cervantes, and C. Espitia. 2001. Molecular analysis of Mycobacterium tuberculosis phosphate specific transport system in Mycobacterium smegmatis. Characterization of recombinant 38 kDa (PstS-1). Microb. Pathog. 30:289-297.
    • (2001) Microb. Pathog. , vol.30 , pp. 289-297
    • Torres, A.1    Juarez, M.D.2    Cervantes, R.3    Espitia, C.4
  • 55
    • 50549190207 scopus 로고
    • Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli
    • Torriani, A. 1959. Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim. Biophys. Acta 38:460-469.
    • (1959) Biochim. Biophys. Acta , vol.38 , pp. 460-469
    • Torriani, A.1
  • 56
    • 0041525975 scopus 로고    scopus 로고
    • A role for the PhoBR regulatory system homologue in the Vibrio cholerae phosphate-limitation response and intestinal colonization
    • von Kruger, W. M., S. Humphreys, and J. M. Ketley. 1999. A role for the PhoBR regulatory system homologue in the Vibrio cholerae phosphate-limitation response and intestinal colonization. Microbiology 145:2463-2475.
    • (1999) Microbiology , vol.145 , pp. 2463-2475
    • Von Kruger, W.M.1    Humphreys, S.2    Ketley, J.M.3
  • 57
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorous assimilation and control of the phosphate regulon
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Wanner, B. L. 1996. Phosphorous assimilation and control of the phosphate regulon, p. 1357-1381. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1357-1381
    • Wanner, B.L.1
  • 58
    • 0026560385 scopus 로고
    • Involvement of phosphotransacetylase, acetate kinase, and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli
    • Wanner, B. L., and M. R. Wilmes Riesenberg. 1992. Involvement of phosphotransacetylase, acetate kinase, and acetyl phosphate synthesis in control of the phosphate regulon in Escherichia coli. J. Bacteriol. 174:2124-2130.
    • (1992) J. Bacteriol. , vol.174 , pp. 2124-2130
    • Wanner, B.L.1    Wilmes Riesenberg, M.R.2
  • 59
    • 0035147498 scopus 로고    scopus 로고
    • The absence of a flagellum leads to altered colony morphology, biofilm development and virulence in Vibrio cholerae O139
    • Watnick, P. I., C. M. Lauriano, K. E. Klose, L. Croal, and R. Kolter. 2001. The absence of a flagellum leads to altered colony morphology, biofilm development and virulence in Vibrio cholerae O139. Mol. Microbiol. 39:223-235.
    • (2001) Mol. Microbiol. , vol.39 , pp. 223-235
    • Watnick, P.I.1    Lauriano, C.M.2    Klose, K.E.3    Croal, L.4    Kolter, R.5
  • 60
    • 4344707142 scopus 로고    scopus 로고
    • The htx and ptx operons of Pseudomonas stutzeri WM88 are new members of the Pho regulon
    • White, A. K., and W. W. Metcalf. 2004. The htx and ptx operons of Pseudomonas stutzeri WM88 are new members of the Pho regulon. J. Bacteriol. 186:5876-5882.
    • (2004) J. Bacteriol. , vol.186 , pp. 5876-5882
    • White, A.K.1    Metcalf, W.W.2
  • 61
    • 3042815976 scopus 로고    scopus 로고
    • Two C-P lyase operons in Pseudomonas stutzeri and their roles in the oxidation of phosphonates, phosphite, and hypophosphite
    • White, A. K., and W. W. Metcalf. 2004. Two C-P lyase operons in Pseudomonas stutzeri and their roles in the oxidation of phosphonates, phosphite, and hypophosphite. J. Bacteriol. 186:4730-4739.
    • (2004) J. Bacteriol. , vol.186 , pp. 4730-4739
    • White, A.K.1    Metcalf, W.W.2
  • 62
    • 0023774276 scopus 로고
    • Gene cloning and expression of the Pseudomonas aeruginosa periplasmic phosphate-binding protein
    • Worobec, E. A., R. J. Siehnel, P. Gladman, and R. E. Hancock. 1988. Gene cloning and expression of the Pseudomonas aeruginosa periplasmic phosphate-binding protein. FEMS Microbiol. Lett. 52:235-238.
    • (1988) FEMS Microbiol. Lett. , vol.52 , pp. 235-238
    • Worobec, E.A.1    Siehnel, R.J.2    Gladman, P.3    Hancock, R.E.4
  • 63
    • 0032924792 scopus 로고    scopus 로고
    • Cloning and characterization of Pseudomonas putida genes encoding the phosphate-specific transport system
    • Wu, H., H. Kosaka, J. Kato, A. Kuroda, T. Ikeda, N. Takiguchi, and H. Ohtake. 1999. Cloning and characterization of Pseudomonas putida genes encoding the phosphate-specific transport system. J. Biosci. Bioeng. 87:273-279.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 273-279
    • Wu, H.1    Kosaka, H.2    Kato, J.3    Kuroda, A.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7
  • 64
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.