메뉴 건너뛰기




Volumn 14, Issue 7, 2012, Pages 1624-1634

A periplasmic arsenite-binding protein involved in regulating arsenite oxidation

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC TRIOXIDE; ARSENITE OXIDASE; ARSENOUS ACID DERIVATIVE; BACTERIAL PROTEIN; OXIDOREDUCTASE; PERIPLASMIC BINDING PROTEIN;

EID: 84859828097     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/j.1462-2920.2011.02672.x     Document Type: Article
Times cited : (80)

References (49)
  • 2
    • 0027104536 scopus 로고
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
    • Anderson, C.L., Williams, J., and Hille, R. (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
    • Anderson, C.L.1    Williams, J.2    Hille, R.3
  • 3
    • 84956588503 scopus 로고
    • A method for the rapid determination of alkaline phosphatase with five cubic millimeters of serum
    • Bessey, O.A., Lowry, O.H., and Brock, M.J. (1946) A method for the rapid determination of alkaline phosphatase with five cubic millimeters of serum. J Biol Chem 164: 321-329.
    • (1946) J Biol Chem , vol.164 , pp. 321-329
    • Bessey, O.A.1    Lowry, O.H.2    Brock, M.J.3
  • 4
    • 36348997984 scopus 로고    scopus 로고
    • Arsenic metabolism in prokaryotic and eukaryotic microbes
    • Nies, D.H., and Silver, S. (eds). Heidelberg, Germany: Springer
    • Bhattacharjee, H., and Rosen, B.P. (2007) Arsenic metabolism in prokaryotic and eukaryotic microbes. In Molecular Microbiology of Heavy Metals. Nies, D.H., and Silver, S. (eds). Heidelberg, Germany: Springer, pp. 371-406.
    • (2007) Molecular Microbiology of Heavy Metals , pp. 371-406
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 5
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer, H.W., and Roulland-Dussoix, D. (1969) A complementation analysis of the restriction and modification of DNA in Escherichia coli. Mol Biol 41: 459-472.
    • (1969) Mol Biol , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 6
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Brunak, S., Emanuelsson, O., Nielsen, H., and von Heijne, G. (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2: 953-971.
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Brunak, S.1    Emanuelsson, O.2    Nielsen, H.3    von Heijne, G.4
  • 7
    • 67349120239 scopus 로고    scopus 로고
    • Novel gene clusters involved in arsenite oxidation and resistance in two arsenite oxidizers: Achromobacter sp. SY8 and Pseudomonas sp. TS44
    • Cai, L., Rensing, C., Li, X., and Wang, G. (2009) Novel gene clusters involved in arsenite oxidation and resistance in two arsenite oxidizers: Achromobacter sp. SY8 and Pseudomonas sp. TS44. Appl Microbiol Biotechnol 83: 715-725.
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 715-725
    • Cai, L.1    Rensing, C.2    Li, X.3    Wang, G.4
  • 8
    • 33845184777 scopus 로고
    • Arsenic speciation in the environment
    • Cullen, W.R., and Reimer, K.J. (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
  • 9
    • 0022518310 scopus 로고
    • Fractionation of Rhizobium leguminosarum cells into outer membrane, cytoplasmic membrane, periplasmic, and cytoplasmic components
    • De Maagd, R.A., and Lugtenberg, B. (1986) Fractionation of Rhizobium leguminosarum cells into outer membrane, cytoplasmic membrane, periplasmic, and cytoplasmic components. J Bacteriol 167: 1083-1085.
    • (1986) J Bacteriol , vol.167 , pp. 1083-1085
    • De Maagd, R.A.1    Lugtenberg, B.2
  • 10
    • 0028878506 scopus 로고
    • Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12
    • De Pina, K., Navarro, C., McWalter, L., Boxer, D.H., Price, N.C., Kelly, S.M., etal. (1995) Purification and characterization of the periplasmic nickel-binding protein NikA of Escherichia coli K12. Eur J Biochem 227: 857-865.
    • (1995) Eur J Biochem , vol.227 , pp. 857-865
    • De Pina, K.1    Navarro, C.2    McWalter, L.3    Boxer, D.H.4    Price, N.C.5    Kelly, S.M.6
  • 11
    • 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., Conrads, T., Hille, R., and Kuhn, P. (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
  • 12
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D.H., and Helinski, D.R. (1979) Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc Natl Acad Sci USA 76: 1648-1652.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 13
    • 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
  • 14
    • 69949097598 scopus 로고    scopus 로고
    • Molecular basis of ChvE function in sugar binding, sugar utilization, and virulence in Agrobacterium tumefaciens
    • He, F., Nair, G.N., Soto, S.C., Chang, Y., Hsu, L., DeGrado, W.F., and Binns, A.N. (2009) Molecular basis of ChvE function in sugar binding, sugar utilization, and virulence in Agrobacterium tumefaciens. J Bacteriol 191: 5802-5813.
    • (2009) J Bacteriol , vol.191 , pp. 5802-5813
    • He, F.1    Nair, G.N.2    Soto, S.C.3    Chang, Y.4    Hsu, L.5    DeGrado, W.F.6    Binns, A.N.7
  • 15
    • 0023928974 scopus 로고
    • Transcending the impenetrable: how proteins come to terms with membranes
    • von Heijne, G. (1988) Transcending the impenetrable: how proteins come to terms with membranes. Biochim Biophys Acta 947: 307-333.
    • (1988) Biochim Biophys Acta , vol.947 , pp. 307-333
    • von Heijne, G.1
  • 16
    • 0011075403 scopus 로고    scopus 로고
    • Arsenic (V)/(III) cycling in soils and natural waters: chemical and microbiological processes
    • Frankenberger, W.F., and Macy, J.M. (eds). New York, USA: Marcell Dekker
    • Inskeep, W.P., McDermott, T.R., and Fendorf, S.E. (2001) Arsenic (V)/(III) cycling in soils and natural waters: chemical and microbiological processes. In Environmental Chemistry of Arsenic. Frankenberger, W.F., and Macy, J.M. (eds). New York, USA: Marcell Dekker, pp. 183-215.
    • (2001) Environmental Chemistry of Arsenic , pp. 183-215
    • Inskeep, W.P.1    McDermott, T.R.2    Fendorf, S.E.3
  • 17
  • 18
    • 32444447338 scopus 로고    scopus 로고
    • + antiporter and a molybdate transporter are essential for arsenite oxidation in Agrobacterium tumefaciens
    • + antiporter and a molybdate transporter are essential for arsenite oxidation in Agrobacterium tumefaciens. J Bacteriol 188: 1577-1584.
    • (2006) J Bacteriol , vol.188 , pp. 1577-1584
    • Kashyap, D.R.1    Botero, L.M.2    Lehr, C.3    Hasset, D.J.4    McDermott, T.R.5
  • 20
    • 0032145466 scopus 로고    scopus 로고
    • Purification and characterization of the respiratory arsenate reductase of Chysiogenes arsenatis
    • Kraft, T., and Macy, J.M. (1998) Purification and characterization of the respiratory arsenate reductase of Chysiogenes arsenatis. Eur J Biochem 255: 647-653.
    • (1998) Eur J Biochem , vol.255 , pp. 647-653
    • Kraft, T.1    Macy, J.M.2
  • 21
    • 1642498273 scopus 로고    scopus 로고
    • Identification of new candidate vaccine antigens made by Streptococcus pyogenes
    • Lei, B., Liu, M., Chesney, G.L., and Musser, J.M. (2004) Identification of new candidate vaccine antigens made by Streptococcus pyogenes. J Infect Dis 189: 79-89.
    • (2004) J Infect Dis , vol.189 , pp. 79-89
    • Lei, B.1    Liu, M.2    Chesney, G.L.3    Musser, J.M.4
  • 22
    • 84855874408 scopus 로고    scopus 로고
    • Unified nomenclature for genes involved in prokaryotic aerobic arsenite oxidation
    • doi:10.1128/JB.06391-11
    • Lett, M.C., Muller, D., Lièvremont, D., Silver, S., and Santini, J. (2011) Unified nomenclature for genes involved in prokaryotic aerobic arsenite oxidation. J Bacteriol doi:10.1128/JB.06391-11.
    • (2011) J Bacteriol
    • Lett, M.C.1    Muller, D.2    Lièvremont, D.3    Silver, S.4    Santini, J.5
  • 23
    • 0015501418 scopus 로고
    • Purification and properties of a component of histidine transport in Salmonella typhimurium
    • Lever, J.E. (1972) Purification and properties of a component of histidine transport in Salmonella typhimurium. J Biol Chem 247: 4317-4326.
    • (1972) J Biol Chem , vol.247 , pp. 4317-4326
    • Lever, J.E.1
  • 24
    • 34447116980 scopus 로고    scopus 로고
    • ArsD residues Cys12, Cys13 and Cys18 form an As(III) binding site required for arsenic metallochaperone activity
    • Lin, Y.F., Yang, J., and Rosen, B.P. (2007) ArsD residues Cys12, Cys13 and Cys18 form an As(III) binding site required for arsenic metallochaperone activity. J Biol Chem 282: 16783-16791.
    • (2007) J Biol Chem , vol.282 , pp. 16783-16791
    • Lin, Y.F.1    Yang, J.2    Rosen, B.P.3
  • 25
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu, Y.G., and Whittier, R.F. (1995) Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25: 674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 26
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke, H., and Quiocho, F.A. (1990) High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 347: 402-406.
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 27
    • 0026710389 scopus 로고
    • Cloning and mutagenesis of the Rhizobium meliloti isocitrate dehydrogenase gene
    • McDermott, T.R., and Kahn, M.L. (1992) Cloning and mutagenesis of the Rhizobium meliloti isocitrate dehydrogenase gene. J Bacteriol 174: 4790-4797.
    • (1992) J Bacteriol , vol.174 , pp. 4790-4797
    • McDermott, T.R.1    Kahn, M.L.2
  • 28
    • 0348046330 scopus 로고    scopus 로고
    • Bacterial populations associated with the oxidation and reduction of arsenic in an unsaturated soil
    • Macur, R.E., Jackson, C.R., Botero, L.M., McDermott, T.R., and Inskeep, W.P. (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    Botero, L.M.3    McDermott, T.R.4    Inskeep, W.P.5
  • 29
    • 37549027623 scopus 로고    scopus 로고
    • Characterization of the arsenate respiratory reductase from Shewanella sp. strain ANA-3
    • Malasarn, D., Keeffe, J.R., and Newman, D.K. (2007) Characterization of the arsenate respiratory reductase from Shewanella sp. strain ANA-3. J Bacteriol 190: 135-142.
    • (2007) J Bacteriol , vol.190 , pp. 135-142
    • Malasarn, D.1    Keeffe, J.R.2    Newman, D.K.3
  • 30
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transduction histidine kinases
    • Mascher, T., Helmann, J.D., and Unden, G. (2006) Stimulus perception in bacterial signal-transduction 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    Unden, G.3
  • 31
  • 32
    • 0031603460 scopus 로고    scopus 로고
    • Prediction of signal peptides and signal anchors by a hidden Markov model
    • Glasgow, J., Littlejohn, T., Major, F., Lathrop, R., Sankoff, D., and Sensen, C. (eds). Menlo Park, CA, USA: AAAI Press Proceedings
    • Nielsen, H., and Krogh, A. (1998) Prediction of signal peptides and signal anchors by a hidden Markov model. In Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology. Glasgow, J., Littlejohn, T., Major, F., Lathrop, R., Sankoff, D., and Sensen, C. (eds). Menlo Park, CA, USA: AAAI Press Proceedings, pp. 122-130.
    • (1998) Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology , pp. 122-130
    • Nielsen, H.1    Krogh, A.2
  • 33
    • 12944320850 scopus 로고    scopus 로고
    • Arsenic, microbes and contaminated aquifers
    • Oremland, R.S., and Stolz, J.F. (2005) Arsenic, microbes and contaminated aquifers. Trends Microbiol 13: 45-49.
    • (2005) Trends Microbiol , vol.13 , pp. 45-49
    • Oremland, R.S.1    Stolz, J.F.2
  • 34
    • 0017175979 scopus 로고
    • Oxidation of arsenite to arsenate by Alcaligenes faecalis
    • Phillips, S.E., and Taylor, M.L. (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
  • 36
    • 0027158657 scopus 로고
    • Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria
    • Quandt, J., and Hynes, M.F. (1993) Versatile suicide vectors which allow direct selection for gene replacement in gram-negative bacteria. Gene 127: 15-21.
    • (1993) Gene , vol.127 , pp. 15-21
    • Quandt, J.1    Hynes, M.F.2
  • 37
    • 33744508953 scopus 로고    scopus 로고
    • Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase
    • Ruan, X., Bhattacharjee, H., and Rosen, B.P. (2006) Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase. J Biol Chem 281: 9925-9934.
    • (2006) J Biol Chem , vol.281 , pp. 9925-9934
    • Ruan, X.1    Bhattacharjee, H.2    Rosen, B.P.3
  • 38
    • 0141591471 scopus 로고    scopus 로고
    • Genetic identification of a respiratory arsenate reductase
    • Saltikov, C., and Newman, D.K. (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
  • 40
    • 1542347232 scopus 로고    scopus 로고
    • Molybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26
    • Santini, G.M., and vanden Hoven, R.N. (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, G.M.1    vanden Hoven, R.N.2
  • 41
    • 78349291126 scopus 로고    scopus 로고
    • Characterization of a two-component signal transduction system that controls arsenite oxidation in the chemolithoautotroph NT-26
    • Sardiwal, S., Santini, J.M., Osborne, T.H., and Djordjevic, S. (2010) Characterization of a two-component signal transduction system that controls arsenite oxidation in the chemolithoautotroph NT-26. FEMS Microbiol Lett 313: 20-28.
    • (2010) FEMS Microbiol Lett , vol.313 , pp. 20-28
    • Sardiwal, S.1    Santini, J.M.2    Osborne, T.H.3    Djordjevic, S.4
  • 42
    • 0028027443 scopus 로고
    • Identification of a putative metal binding site in a new family of metalloregulatory proteins
    • Shi, W., Wu, J., and Rosen, B.P. (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
  • 43
    • 0021085146 scopus 로고
    • Cloning of the glutamine synthetase I gene from Rhizobium meliloti
    • Somerville, J.E., and Kahn, M.L. (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
  • 45
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F.W. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol 219: 37-44.
    • (1991) J Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 46
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and Saier, M.H., Jr (1993) Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 57: 320-346.
    • (1993) Microbiol Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier Jr., M.H.2
  • 47
    • 0031574072 scopus 로고    scopus 로고
    • The clustal_x windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., and Higgins, D.G. (1997) The clustal_x windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 48
    • 0003338719 scopus 로고    scopus 로고
    • Phosphorus assimilation and control of the phosphate regulon
    • 2nd edn. Neidhardt, F.C., Curtis, R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., eds). Washington, DC, USA: ASM Press
    • Wanner, B.L. (1996) Phosphorus assimilation and control of the phosphate regulon. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn. Neidhardt, F.C., Curtis, R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., etal. (eds). Washington, DC, USA: ASM Press, pp. 1357-1381.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1357-1381
    • Wanner, B.L.1
  • 49
    • 77954399547 scopus 로고    scopus 로고
    • Identification of a novel arsenite oxidase gene, arxA, in the haloalkaliphilic, arsenite-oxidizing bacterium Alkalilimnicola ehrlichii strain MLHE-1
    • Zargar, K., Hoeft, S., Oremland, R.S., and Saltikov, C. (2010) Identification of a novel arsenite oxidase gene, arxA, in the haloalkaliphilic, arsenite-oxidizing bacterium Alkalilimnicola ehrlichii strain MLHE-1. J Bacteriol 192: 3755-3762.
    • (2010) J Bacteriol , vol.192 , pp. 3755-3762
    • Zargar, K.1    Hoeft, S.2    Oremland, R.S.3    Saltikov, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.