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Volumn 188, Issue 3, 2006, Pages 1081-1088

Complex regulation of arsenite oxidation in Agrobacterium tumefaciens

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC TRIOXIDE; CARCINOGEN; DNA; RNA;

EID: 31344478245     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.3.1081-1088.2006     Document Type: Article
Times cited : (157)

References (44)
  • 1
    • 0024799191 scopus 로고
    • Prokaryotic signal transduction mediated by sensor and regulator protein pairs
    • Albright, L. M., E. Huala, and F. M. Ausubel. 1989. Prokaryotic signal transduction mediated by sensor and regulator protein pairs. Annu. Rev. Genet. 23:311-336.
    • (1989) Annu. Rev. Genet. , vol.23 , pp. 311-336
    • Albright, L.M.1    Huala, E.2    Ausubel, F.M.3
  • 3
    • 0027104536 scopus 로고
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
    • Andersen, G. L., J. Williams, and R. Hille. 1992. The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase. J. Biol. Chem. 267:23674-23682.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23674-23682
    • Andersen, G.L.1    Williams, J.2    Hille, R.3
  • 4
    • 0026658877 scopus 로고
    • The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, and P. Courvalin. 1992. The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J. Bacteriol. 174:2582-2591.
    • (1992) J. Bacteriol. , vol.174 , pp. 2582-2591
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 5
    • 0036952670 scopus 로고    scopus 로고
    • The divergent chromosomal ars operon of Acidithiobacillus ferrooxidans is regulated by an atypical ArsR protein
    • Butcher, B. G., and D. E. Rawlings. 2002. The divergent chromosomal ars operon of Acidithiobacillus ferrooxidans is regulated by an atypical ArsR protein. Microbiology 148:3983-3992.
    • (2002) Microbiology , vol.148 , pp. 3983-3992
    • Butcher, B.G.1    Rawlings, D.E.2
  • 6
    • 33845184777 scopus 로고
    • Arsenic speciation in the environment
    • Cullen, W. R., and K. J. Reimer. 1989. Arsenic speciation in the environment. Chem. Rev. 89:713-764.
    • (1989) Chem. Rev. , vol.89 , pp. 713-764
    • Cullen, W.R.1    Reimer, K.J.2
  • 7
    • 1642348622 scopus 로고    scopus 로고
    • Arsenite-oxidizing Hydrogenobaculum sp. isolated from an acid-sulfate-chloride geothermal spring in Yellowstone National Park
    • Donahoe-Christiansen, J., C. R. Jackson, S. D'Imperio, W. P. Inskeep, and T. R. McDermott. 2004. Arsenite-oxidizing Hydrogenobaculum sp. isolated from an acid-sulfate-chloride geothermal spring in Yellowstone National Park. Appl. Environ. Microbiol. 70:1865-1868.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1865-1868
    • Donahoe-Christiansen, J.1    Jackson, C.R.2    D'Imperio, S.3    Inskeep, W.P.4    McDermott, T.R.5
  • 8
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100kDa arsenite oxidase from Alcalingenes faecalis in two crystal forms at 1.64 Å and 2.03 Å
    • Ellis, P. J., T. Conrads, R. Hille, and P. Kuhn. 2001. Crystal structure of the 100kDa arsenite oxidase from Alcalingenes faecalis in two crystal forms at 1.64 Å and 2.03 Å. Structure 9:125-132.
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 10
    • 0000292096 scopus 로고    scopus 로고
    • Quorum sensing in gram-negative bacteria
    • Greenberg, E. P. 1997. Quorum sensing in gram-negative bacteria. ASM News 63:371-377.
    • (1997) ASM News , vol.63 , pp. 371-377
    • Greenberg, E.P.1
  • 11
    • 0002284129 scopus 로고    scopus 로고
    • General genetic knowledge
    • H. P. Spain, A. Kondorosi, and P. J. J. Hooykaas (ed.). Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Hynes, M. F., and T. M. Finan. 1998. General genetic knowledge, p. 25-43. In H. P. Spain, A. Kondorosi, and P. J. J. Hooykaas (ed.), The Rhizobiaceae, molecular biology of model plant-associated bacteria. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1998) The Rhizobiaceae, Molecular Biology of Model Plant-associated Bacteria , pp. 25-43
    • Hynes, M.F.1    Finan, T.M.2
  • 16
    • 0348046330 scopus 로고    scopus 로고
    • Bacterial populations associated with the oxidation and reduction of arsenic in an unsaturated soil
    • Macur, R. E., C. R. Jackson, T. R. McDermott, and W. P. Inskeep. 2004. Bacterial populations associated with the oxidation and reduction of arsenic in an unsaturated soil. Environ. Sci. Technol. 38:104-111.
    • (2004) Environ. Sci. Technol. , vol.38 , pp. 104-111
    • Macur, R.E.1    Jackson, C.R.2    McDermott, T.R.3    Inskeep, W.P.4
  • 17
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain
    • Monson, E. K., M. Weinstein, G. S. Ditta, and D. R. Helinski. 1992. The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain. Proc. Natl. Acad. Sci. USA 89:4280-4284.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 19
    • 0024075833 scopus 로고
    • Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis
    • Nohno, T., Y. Kasai, and T. Saito. 1988. Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis. J. Bacteriol. 170:4097-4102.
    • (1988) J. Bacteriol. , vol.170 , pp. 4097-4102
    • Nohno, T.1    Kasai, Y.2    Saito, T.3
  • 21
    • 0037656045 scopus 로고    scopus 로고
    • The ecology of arsenic
    • Oremland, R. S., and J. F. Stolz. 2003. The ecology of arsenic. Science 300:939-944.
    • (2003) Science , vol.300 , pp. 939-944
    • Oremland, R.S.1    Stolz, J.F.2
  • 22
    • 0036794790 scopus 로고    scopus 로고
    • Anaerobic oxidation of arsenite in Mono Lake water by a facultative, arsenite-oxidizing chemoautotroph, strain MLHE-1
    • Oremland, R. S., S. E. Hoft, J. M. Santini, N. Bano, R. A. Hollibaugh, and J. T. Hollibaugh. 2002. Anaerobic oxidation of arsenite in Mono Lake water by a facultative, arsenite-oxidizing chemoautotroph, strain MLHE-1. Appl. Environ. Microbiol. 68:4795-4802.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4795-4802
    • Oremland, R.S.1    Hoft, S.E.2    Santini, J.M.3    Bano, N.4    Hollibaugh, R.A.5    Hollibaugh, J.T.6
  • 23
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 25
    • 0017175979 scopus 로고
    • Oxidation of arsenite to arsenate by Alcaligenes faecalis
    • Phillips, S. E., and M. L. Taylor. 1976. Oxidation of arsenite to arsenate by Alcaligenes faecalis. Appl. Environ. Microbiol. 32:392-399.
    • (1976) Appl. Environ. Microbiol. , vol.32 , pp. 392-399
    • Phillips, S.E.1    Taylor, M.L.2
  • 26
    • 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
  • 28
    • 0141591471 scopus 로고    scopus 로고
    • Genetic identification of a respiratory arsenate reductase
    • Saltikov, C., and D. K. Newman. 2003. Genetic identification of a respiratory arsenate reductase. Proc. Natl. Acad. Sci. USA 100:10983-10988.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10983-10988
    • Saltikov, C.1    Newman, D.K.2
  • 30
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • 28a. Sanders, O. I., C. Rensing, M. Kuroda, B. Mitra, and B. P. Rosen. 1997. Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli. J. Bacteriol. 179:3365-3367.
    • (1997) J. Bacteriol. , vol.179 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 31
    • 1542347232 scopus 로고    scopus 로고
    • Molybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26
    • Santini, J. M., and R. N. vanden Hoven. 2004. Molybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26. J. Bacteriol. 186:1614-1619.
    • (2004) J. Bacteriol. , vol.186 , pp. 1614-1619
    • Santini, J.M.1    Vanden Hoven, R.N.2
  • 32
    • 0033987849 scopus 로고    scopus 로고
    • A new chemolithoautotrophic arsenite-oxidizing bacterium isolated from a gold mine: Phylogenetic, physiological, and preliminary biochemical studies
    • Santini, J. M., L. I. Sly, R. D. Schnagl, and J. M. Macy. 2000. A new chemolithoautotrophic arsenite-oxidizing bacterium isolated from a gold mine: phylogenetic, physiological, and preliminary biochemical studies. Appl. Environ. Microbiol. 66:92-97.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 92-97
    • Santini, J.M.1    Sly, L.I.2    Schnagl, R.D.3    Macy, J.M.4
  • 33
    • 0028027443 scopus 로고
    • Identification of a putative metal binding site in a new family of metalloregulatory proteins
    • Shi, W., J. Wu, and B. P. Rosen. 1994. Identification of a putative metal binding site in a new family of metalloregulatory proteins. J. Biol. Chem. 269:19826-19829.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19826-19829
    • Shi, W.1    Wu, J.2    Rosen, B.P.3
  • 34
    • 13544263302 scopus 로고    scopus 로고
    • Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic
    • Silver, S., and L. T. Phung. 2005. Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic. Appl. Environ. Microbiol. 71:599-608.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 599-608
    • Silver, S.1    Phung, L.T.2
  • 35
    • 0009981284 scopus 로고    scopus 로고
    • Arsenic metabolism: Resistance, reduction, and oxidation
    • W. F. Frankenberger, Jr., and J. M. Macy (ed.). Marcel Dekker, New York, N.Y.
    • Silver, S., L. T. Phung, and B. P. Rosen. 2002. Arsenic metabolism: resistance, reduction, and oxidation, p. 247-272. In W. F. Frankenberger, Jr., and J. M. Macy (ed.), Environmental chemistry of arsenic. Marcel Dekker, New York, N.Y.
    • (2002) Environmental Chemistry of Arsenic , pp. 247-272
    • Silver, S.1    Phung, L.T.2    Rosen, B.P.3
  • 36
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. BioTechnology 1:784-791.
    • (1983) BioTechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 37
    • 0021085146 scopus 로고
    • Cloning of the glutamine synthetase I gene from Rhizobium meliloti
    • Somerville, J. E., and M. L. Kahn. 1983. Cloning of the glutamine synthetase I gene from Rhizobium meliloti. J. Bacteriol. 156:168-176.
    • (1983) J. Bacteriol. , vol.156 , pp. 168-176
    • Somerville, J.E.1    Kahn, M.L.2
  • 38
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis
    • J. A. Hoch and T. J. Silhavy (ed.), ASM Press, Washington, D.C.
    • Stock, J. B., M. G. Surette, M. Levit, and P. Park. 1995. Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis, p. 25-51. In J. A. Hoch and T. J. Silhavy (ed.), Two-component transduction, ASM Press, Washington, D.C.
    • (1995) Two-component Transduction , pp. 25-51
    • Stock, J.B.1    Surette, M.G.2    Levit, M.3    Park, P.4
  • 39
    • 0032213669 scopus 로고    scopus 로고
    • Expression and regulation of phosphate starvation inducible genes in Rhizobium meliloti
    • Summers, M. L., J. G. Elkins, B. Elliot, and T. R. McDermott. 1998. Expression and regulation of phosphate starvation inducible genes in Rhizobium meliloti. Mol. Plant-Microbe Interact. 11:1094-1101.
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 1094-1101
    • Summers, M.L.1    Elkins, J.G.2    Elliot, B.3    McDermott, T.R.4
  • 40
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 2642547186 scopus 로고    scopus 로고
    • Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: The arsenite oxidase and its physiological electron acceptor
    • vanden Hoven, R. N., and J. M. Santini. 2004. Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor. Biochim. Biophys. Acta 1656:148-155.
    • (2004) Biochim. Biophys. Acta , vol.1656 , pp. 148-155
    • Vanden Hoven, R.N.1    Santini, J.M.2
  • 42
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • Volz, K. 1993. Structural conservation in the CheY superfamily. Biochemistry 32:11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 43
    • 0001331296 scopus 로고
    • Signal transduction and cross regulation in the Escherichia coli phosphate regulon by PhoR, CreC, and acetyl phosphate
    • J. A. Hoch and T. J. Silhavy (ed.). ASM Press, Washington, D.C.
    • Wanner, B. L. 1995. Signal transduction and cross regulation in the Escherichia coli phosphate regulon by PhoR, CreC, and acetyl phosphate, p. 203-221. In J. A. Hoch and T. J. Silhavy (ed.), Two-component signal transduction. ASM Press, Washington, D.C.
    • (1995) Two-component Signal Transduction , pp. 203-221
    • Wanner, B.L.1
  • 44
    • 0037007116 scopus 로고    scopus 로고
    • Genetic control of quorum-sensing signal turnover in Agrobacterium tumefaciens
    • Zhang, H.-B., L.-H. Wang, and L.-H. Zhang. 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


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