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Volumn 191, Issue 16, 2009, Pages 5304-5311

Site-directed mutagenesis identifies a molecular switch involved in copper sensing by the histidine kinase CinS in Pseudomonas putida KT2440

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; HISTIDINE KINASE CINR; HISTIDINE KINASE CINS; PROTEIN HISTIDINE KINASE; SILVER; UNCLASSIFIED DRUG;

EID: 67749085995     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00551-09     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modeling
    • Arnold, K., L. Bordoli, J. Kopp, and T. Schwede. 2006. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 2
    • 0029848731 scopus 로고    scopus 로고
    • Copper toxicity towards Saccharomyces cerevisiae: Dependence on plasma membrane fatty acid composition
    • Avery, S. V., N. G. Howlett, and S. Radice. 1996. Copper toxicity towards Saccharomyces cerevisiae: dependence on plasma membrane fatty acid composition. Appl. Environ. Microbiol. 62:3960-3966.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3960-3966
    • Avery, S.V.1    Howlett, N.G.2    Radice, S.3
  • 3
    • 67749135985 scopus 로고    scopus 로고
    • Bachamann, B. J. 1996. Derivations and genotypes of some mutant derivatives of E. coli K-12, p. 2460-2488. In F. C. Neidhart (ed.), Escherichia coli and Salmonella typhimurium. American Society for Microbiology, Washington, DC.
    • Bachamann, B. J. 1996. Derivations and genotypes of some mutant derivatives of E. coli K-12, p. 2460-2488. In F. C. Neidhart (ed.), Escherichia coli and Salmonella typhimurium. American Society for Microbiology, Washington, DC.
  • 4
    • 0019847407 scopus 로고    scopus 로고
    • Tyr does not. Nature 294:188-190.
    • Tyr does not. Nature 294:188-190.
  • 5
    • 34347383571 scopus 로고    scopus 로고
    • A copper-activated two-component system interacts with zinc and imipenem resistance in Pseudomonas aeruginosa
    • Caille, O., C. Rossier, and K. Perron. 2007. A copper-activated two-component system interacts with zinc and imipenem resistance in Pseudomonas aeruginosa J. Bacteriol. 189:4561-4568.
    • (2007) J. Bacteriol , vol.189 , pp. 4561-4568
    • Caille, O.1    Rossier, C.2    Perron, K.3
  • 6
    • 0347567163 scopus 로고    scopus 로고
    • Heavy metal tolerance and metal homeostasis in Pseudomonas putida as revealed by complete genome analysis
    • Canovas, D., I. Cases, and V. de Lorenzo. 2003. Heavy metal tolerance and metal homeostasis in Pseudomonas putida as revealed by complete genome analysis. Environ. Microbiol. 12:1242-1256.
    • (2003) Environ. Microbiol , vol.12 , pp. 1242-1256
    • Canovas, D.1    Cases, I.2    de Lorenzo, V.3
  • 7
    • 0026094746 scopus 로고
    • Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins
    • Cha, J. S., and D. A. Cooksey. 1991. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc. Natl. Acad. Sci. USA 88:8915-8919.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8915-8919
    • Cha, J.S.1    Cooksey, D.A.2
  • 9
    • 64149100329 scopus 로고    scopus 로고
    • Genes involved in copper resistance influence survival of Pseudomonas aeruginosa on copper surfaces
    • Elguindi, J., J. Wagner, and C. Rensing. 2009. Genes involved in copper resistance influence survival of Pseudomonas aeruginosa on copper surfaces. J. Appl. Microbiol. 106:1448-1455.
    • (2009) J. Appl. Microbiol , vol.106 , pp. 1448-1455
    • Elguindi, J.1    Wagner, J.2    Rensing, C.3
  • 10
    • 0034741261 scopus 로고    scopus 로고
    • Escherichia coli CopA N-terminal Cys(X)(2)Cys motif are not required for copper resistance or transport
    • Fan, B., G. Grass, C. Rensing, and B. P. Rosen. 2001. Escherichia coli CopA N-terminal Cys(X)(2)Cys motif are not required for copper resistance or transport. Biochem. Biophys. Res. Commun. 286:414-418.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 414-418
    • Fan, B.1    Grass, G.2    Rensing, C.3    Rosen, B.P.4
  • 11
    • 0035047623 scopus 로고    scopus 로고
    • The product of ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions
    • Franke, S., G. Grass, and D. H. Nies. 2001. The product of ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions. Microbiology 147:965-972.
    • (2001) Microbiology , vol.147 , pp. 965-972
    • Franke, S.1    Grass, G.2    Nies, D.H.3
  • 12
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli
    • Franke, S., G. Grass, C. Rensing, and D. H. Nies. 2003. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J. Bacteriol. 185:3804-3812.
    • (2003) J. Bacteriol , vol.185 , pp. 3804-3812
    • Franke, S.1    Grass, G.2    Rensing, C.3    Nies, D.H.4
  • 14
    • 0024598644 scopus 로고
    • Mutations in the Escherichia coli fnr and tgt genes: Control of molybdate reductase activity and the cytochrome d complex by fnr
    • Frey, B., G. Jänel, U. Michelsen, and H. Kersten. 1989. Mutations in the Escherichia coli fnr and tgt genes: control of molybdate reductase activity and the cytochrome d complex by fnr. J. Bacteriol. 171:1524-1530.
    • (1989) J. Bacteriol , vol.171 , pp. 1524-1530
    • Frey, B.1    Jänel, G.2    Michelsen, U.3    Kersten, H.4
  • 15
    • 0038290306 scopus 로고    scopus 로고
    • Identification of basic amino acid residues important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA
    • Gerharz, T., S. Reinelt, S. Kaspar, L. Scapozza, and M. Bott. 2003. Identification of basic amino acid residues important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA. Biochemistry 42:5917-5924.
    • (2003) Biochemistry , vol.42 , pp. 5917-5924
    • Gerharz, T.1    Reinelt, S.2    Kaspar, S.3    Scapozza, L.4    Bott, M.5
  • 16
    • 0034817086 scopus 로고    scopus 로고
    • CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
    • Grass, G., and C. Rensing. 2001. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286:902-908.
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 902-908
    • Grass, G.1    Rensing, C.2
  • 17
    • 0032884944 scopus 로고    scopus 로고
    • Identification of a gene cluster, czr, involved in cadmium and zinc resistance in Pseudomonas aeruginosa
    • Hassan, M. T., D. van der Lelie, D. Springael, U. Römling, N. Ahmed, and M. Mergeay. 1999. Identification of a gene cluster, czr, involved in cadmium and zinc resistance in Pseudomonas aeruginosa. Gene 238:417-425.
    • (1999) Gene , vol.238 , pp. 417-425
    • Hassan, M.T.1    van der Lelie, D.2    Springael, D.3    Römling, U.4    Ahmed, N.5    Mergeay, M.6
  • 19
    • 20144380866 scopus 로고    scopus 로고
    • The nature of the stimulus and of the fumarate binding site of the fumarate sensor DcuS of Escherichia coli
    • Kneuper, H., I. G. Janausch, V. Vijayan, M. Zweckstetter, V. Bock, C. Griesinger, and G. Unden. 2005. The nature of the stimulus and of the fumarate binding site of the fumarate sensor DcuS of Escherichia coli. J. Biol. Chem. 280:20596-20603.
    • (2005) J. Biol. Chem , vol.280 , pp. 20596-20603
    • Kneuper, H.1    Janausch, I.G.2    Vijayan, V.3    Zweckstetter, M.4    Bock, V.5    Griesinger, C.6    Unden, G.7
  • 20
    • 0042367660 scopus 로고    scopus 로고
    • The role of reactive oxygen species in copper-induced permeability of plasma membranes in Escherichia coli
    • Lebedev, V. S., A. V. Veselovskii, E. Deinega, and I. Fedorov. 2002. The role of reactive oxygen species in copper-induced permeability of plasma membranes in Escherichia coli. Biofizika 47:295-299.
    • (2002) Biofizika , vol.47 , pp. 295-299
    • Lebedev, V.S.1    Veselovskii, A.V.2    Deinega, E.3    Fedorov, I.4
  • 21
    • 34748859338 scopus 로고    scopus 로고
    • Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy
    • Loftin, I. R., S. Franke, N. J. Blackburn, and M. M. McEvoy. 2007. Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Sci. 16:2287-2293.
    • (2007) Protein Sci , vol.16 , pp. 2287-2293
    • Loftin, I.R.1    Franke, S.2    Blackburn, N.J.3    McEvoy, M.M.4
  • 22
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L., C. Rensing, and J. A. Imlay. 2007. Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J. Bacteriol. 189:1616-1626.
    • (2007) J. Bacteriol , vol.189 , pp. 1616-1626
    • Macomber, L.1    Rensing, C.2    Imlay, J.A.3
  • 23
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L., and J. A. Imlay. 2009. The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc. Natl. Acad. Sci. USA 106:8344-8349.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 24
    • 41949095282 scopus 로고    scopus 로고
    • Altering the ratio of phenazines in Pseudomonas chlororaphis (aureofaciens) strain 30-84: Effects on biofilm formation and pathogen inhibition
    • Maddula, V. S., E. A. Pierson, and L. S. Pierson III. 2008. Altering the ratio of phenazines in Pseudomonas chlororaphis (aureofaciens) strain 30-84: effects on biofilm formation and pathogen inhibition. J. Bacteriol. 190:2759-2766.
    • (2008) J. Bacteriol , vol.190 , pp. 2759-2766
    • Maddula, V.S.1    Pierson, E.A.2    Pierson III, L.S.3
  • 25
    • 53149124088 scopus 로고    scopus 로고
    • Microbial reporters of metal bioavailability
    • Magrisso, S., Y. Erel, and S. Belkin. 2008. Microbial reporters of metal bioavailability. Microb. Biotechnol. 1:320-330.
    • (2008) Microb. Biotechnol , vol.1 , pp. 320-330
    • Magrisso, S.1    Erel, Y.2    Belkin, S.3
  • 26
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher, T., J. D. Helmann, and U. Gottfried. 2006. Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol. Mol. Biol. Rev. 70:910-938.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Gottfried, U.3
  • 27
    • 0021925630 scopus 로고
    • Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals
    • Mergeay, M., D. H. Nies, H. G. Schlegel, J. Geritas, P. Charles, and F. van Gijsegen. 1985. Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals. J. Bacteriol. 162:328-334.
    • (1985) J. Bacteriol , vol.162 , pp. 328-334
    • Mergeay, M.1    Nies, D.H.2    Schlegel, H.G.3    Geritas, J.4    Charles, P.5    van Gijsegen, F.6
  • 28
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics, p.352-355. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics , pp. 352-355
    • Miller, J.H.1
  • 29
    • 0033735452 scopus 로고    scopus 로고
    • Improved gfp and inaZ broad-host-range promoter-probe vectors
    • Miller, W. G., J. H. J. Leveau, and S. E. Lindow. 2000. Improved gfp and inaZ broad-host-range promoter-probe vectors. Mol. Plant-Microbe Interact. 13:1243-1250.
    • (2000) Mol. Plant-Microbe Interact , vol.13 , pp. 1243-1250
    • Miller, W.G.1    Leveau, J.H.J.2    Lindow, S.E.3
  • 30
    • 0028101364 scopus 로고
    • Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae
    • Mills, S. D., C. K. Lim, and D. A. Cooksey. 1994. Purification and characterization of CopR, a transcriptional activator protein that binds to a conserved domain (cop box) in copper-inducible promoters of Pseudomonas syringae. Mol. Gen. Genet. 244:341-351.
    • (1994) Mol. Gen. Genet , vol.244 , pp. 341-351
    • Mills, S.D.1    Lim, C.K.2    Cooksey, D.A.3
  • 31
    • 0033813832 scopus 로고    scopus 로고
    • Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12
    • Munson, G. P., D. L. Lam, F. W. Outten, and T. V. O'Halloran. 2000. Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12. J. Bacteriol. 182:5864-5871.
    • (2000) J. Bacteriol , vol.182 , pp. 5864-5871
    • Munson, G.P.1    Lam, D.L.2    Outten, F.W.3    O'Halloran, T.V.4
  • 32
    • 0035903128 scopus 로고    scopus 로고
    • The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
    • Outten, F. W., D. L. Huffman, J. A. Hale, and T. V. O'Halloran. 2001. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J. Biol. Chem. 276:30670-30677.
    • (2001) J. Biol. Chem , vol.276 , pp. 30670-30677
    • Outten, F.W.1    Huffman, D.L.2    Hale, J.A.3    O'Halloran, T.V.4
  • 33
    • 0141531993 scopus 로고    scopus 로고
    • The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli
    • Pappalardo, L., I. G. Janausch, V. Vijayan, E. Zientz, J. Junker, W. Peti, M. Zweckstetter, G. Uden, and C. Griesinger. 2003. The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. J. Biol. Chem. 278:39185-39188.
    • (2003) J. Biol. Chem , vol.278 , pp. 39185-39188
    • Pappalardo, L.1    Janausch, I.G.2    Vijayan, V.3    Zientz, E.4    Junker, J.5    Peti, W.6    Zweckstetter, M.7    Uden, G.8    Griesinger, C.9
  • 34
    • 34447558542 scopus 로고    scopus 로고
    • The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a preQ0 reductase in Pseuomonas putida KT2440
    • Quaranta, D., R. McCarty, V. Bandarian, and C. Rensing. 2007. The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a preQ0 reductase in Pseuomonas putida KT2440. J. Bacteriol. 189:5361-5371.
    • (2007) J. Bacteriol , vol.189 , pp. 5361-5371
    • Quaranta, D.1    McCarty, R.2    Bandarian, V.3    Rensing, C.4
  • 35
    • 0141643091 scopus 로고    scopus 로고
    • The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain
    • Reinelt, S., E. Hofmann, T. Gerharz, M. Bott, and D. R. Madden. 2003. The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain. J. Biol. Chem. 278:39189-39196.
    • (2003) J. Biol. Chem , vol.278 , pp. 39189-39196
    • Reinelt, S.1    Hofmann, E.2    Gerharz, T.3    Bott, M.4    Madden, D.R.5
  • 37
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing, C., and G. Grass. 2003. Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol. Rev. 27:197-213.
    • (2003) FEMS Microbiol. Rev , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 39
    • 0030995871 scopus 로고    scopus 로고
    • Copper inducible transcription regulation of two promoters in Escherichia coli copper resistance determinant pco
    • Rouch, D. A., and N. L. Brown. 1997. Copper inducible transcription regulation of two promoters in Escherichia coli copper resistance determinant pco. Microbiology 143:1191-1202.
    • (1997) Microbiology , vol.143 , pp. 1191-1202
    • Rouch, D.A.1    Brown, N.L.2
  • 41
    • 33749627682 scopus 로고    scopus 로고
    • Survival and growth in the presence of elevated copper: Transcriptional profiling of copper-stressed Pseudomonas aeruginosa
    • Teitzel, G. M., A. Geddie, S. K. De Long, M. J. Kirisits, M. Whiteley, and M. R. Parsek. 2006. Survival and growth in the presence of elevated copper: transcriptional profiling of copper-stressed Pseudomonas aeruginosa. J. Bacteriol. 20:7242-7256.
    • (2006) J. Bacteriol , vol.20 , pp. 7242-7256
    • Teitzel, G.M.1    Geddie, A.2    De Long, S.K.3    Kirisits, M.J.4    Whiteley, M.5    Parsek, M.R.6
  • 42
    • 0036937672 scopus 로고    scopus 로고
    • Pseudomonas putida: A cosmopolitan opportunist par excellence
    • Timmis, K. N. 2002. Pseudomonas putida: a cosmopolitan opportunist par excellence. Environ. Microbiol. 4:779-781.
    • (2002) Environ. Microbiol , vol.4 , pp. 779-781
    • Timmis, K.N.1
  • 43
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnády, G. E., and I. Simon. 2001. The HMMTOP transmembrane topology prediction server. Bioinformatics 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 44
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron, K. J., and N. J. Robinson. 2009. How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol. 7:25-35.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2


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