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Volumn 187, Issue 18, 2005, Pages 6317-6323

Complex transcriptional control links NikABCDE-dependent nickel transport with hydrogenase expression in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; FUMARIC ACID; HYDROGENASE; NICKEL; NICKEL IRON HYDROGENASE; OXYGEN; PROTEIN NIKABCDE; UNCLASSIFIED DRUG;

EID: 24944576101     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.18.6317-6323.2005     Document Type: Article
Times cited : (80)

References (46)
  • 1
    • 0022254333 scopus 로고
    • Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12
    • Ballantine, S. P., and D. H. Boxer. 1985. Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J. Bacteriol. 163:454-459.
    • (1985) J. Bacteriol. , vol.163 , pp. 454-459
    • Ballantine, S.P.1    Boxer, D.H.2
  • 2
    • 0024713468 scopus 로고
    • Nitrate reductase of Escherichia coli: Completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer
    • Blasco, F., C. Iohbi, G. Giordano, M. Chippaux, and V. Bonnefoy. 1989. Nitrate reductase of Escherichia coli: completion of the nucleotide sequence of the nar operon and reassessment of the role of the alpha and beta subunits in iron binding and electron transfer. Mol. Gen. Genet. 218:249-256.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 249-256
    • Blasco, F.1    Iohbi, C.2    Giordano, G.3    Chippaux, M.4    Bonnefoy, V.5
  • 4
    • 3543072246 scopus 로고    scopus 로고
    • Metal-selective DNA-binding response of Escherichia coli NikR
    • Bloom, S. L., and D. B. Zambie. 2004. Metal-selective DNA-binding response of Escherichia coli NikR. Biochemistry 43:10029-10038.
    • (2004) Biochemistry , vol.43 , pp. 10029-10038
    • Bloom, S.L.1    Zambie, D.B.2
  • 5
    • 0027980255 scopus 로고
    • Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli
    • Brøndsted, L., and T. Atlung. 1994. Anaerobic regulation of the hydrogenase 1 (hya) operon of Escherichia coli. J. Bacteriol. 176:5423-5428.
    • (1994) J. Bacteriol. , vol.176 , pp. 5423-5428
    • Brøndsted, L.1    Atlung, T.2
  • 6
    • 0742333984 scopus 로고    scopus 로고
    • A motif co-occurrence approach for genome-wide prediction of transcription-factor-binding sites in Escherichia coli
    • Bulyk, M. L., A. M. McGuire, N. Masuda, and G. M. Church. 2004. A motif co-occurrence approach for genome-wide prediction of transcription-factor- binding sites in Escherichia coli. Genome Res. 14:201-208.
    • (2004) Genome Res. , vol.14 , pp. 201-208
    • Bulyk, M.L.1    McGuire, A.M.2    Masuda, N.3    Church, G.M.4
  • 8
    • 0036774881 scopus 로고    scopus 로고
    • NikR repressor: High-affinity nickel binding to the C-terminal domain regulates binding to operator DNA
    • Chivers, P. T., and R. T. Sauer. 2002. NikR repressor: high-affinity nickel binding to the C-terminal domain regulates binding to operator DNA. Chem. Biol. 9:1141-1148.
    • (2002) Chem. Biol. , vol.9 , pp. 1141-1148
    • Chivers, P.T.1    Sauer, R.T.2
  • 9
    • 0034733505 scopus 로고    scopus 로고
    • Regulation of high affinity nickel uptake in bacteria. Ni2+-depcndcnt interaction of NikR with wild-type and mutant operator sites
    • Chivers, P. T., and R. T. Sauer. 2000. Regulation of high affinity nickel uptake in bacteria. Ni2+-depcndcnt interaction of NikR with wild-type and mutant operator sites. J. Biol. Chem. 275:19735-19741.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19735-19741
    • Chivers, P.T.1    Sauer, R.T.2
  • 10
    • 0026056114 scopus 로고
    • Anaerobically expressed Escherichia coli genes identified by operon fusion techniques
    • Choe, M., and W. S. Reznikoff. 1991. Anaerobically expressed Escherichia coli genes identified by operon fusion techniques. J. Bacteriol. 173:6139-6146.
    • (1991) J. Bacteriol. , vol.173 , pp. 6139-6146
    • Choe, M.1    Reznikoff, W.S.2
  • 11
    • 0032537553 scopus 로고    scopus 로고
    • Overproduction and characterization of a dimeric nonzinc glyoxalase I from Escherichia coli: Evidence for optimal activation by nickel ions
    • Clugston, S. L., J. F. Barnard, R. Kinach, D. Miedema, R. Ruman, E. Daub, and J. F. Honek. 1998. Overproduction and characterization of a dimeric nonzinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions. Biochemistry 37:8754-8763.
    • (1998) Biochemistry , vol.37 , pp. 8754-8763
    • Clugston, S.L.1    Barnard, J.F.2    Kinach, R.3    Miedema, D.4    Ruman, R.5    Daub, E.6    Honek, J.F.7
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K., and B. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.1    Wanner, B.2
  • 13
    • 0034631704 scopus 로고    scopus 로고
    • XAS investigation of the nickel active site structure in Escherichia coli glyoxalase I
    • Davidson, G., S. L. Clugston, J. F. Honek, and M. J. Maroney. 2000. XAS investigation of the nickel active site structure in Escherichia coli glyoxalase I. Inorg. Chem. 39:2962-2963.
    • (2000) Inorg. Chem. , vol.39 , pp. 2962-2963
    • Davidson, G.1    Clugston, S.L.2    Honek, J.F.3    Maroney, M.J.4
  • 14
    • 0034108232 scopus 로고    scopus 로고
    • Regulation of biological nitrogen fixation
    • Halhleih, C. M., and P. W. Ludden. 2000. Regulation of biological nitrogen fixation. J. Nutr. 130:1081-1084.
    • (2000) J. Nutr. , vol.130 , pp. 1081-1084
    • Halhleih, C.M.1    Ludden, P.W.2
  • 15
    • 0034254431 scopus 로고    scopus 로고
    • Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation
    • He, M. M., S. L. Clugston, J. F. Honek, and B. W. Matthews. 2000. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry 39:8719-8727.
    • (2000) Biochemistry , vol.39 , pp. 8719-8727
    • He, M.M.1    Clugston, S.L.2    Honek, J.F.3    Matthews, B.W.4
  • 16
    • 0030014740 scopus 로고    scopus 로고
    • High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli
    • Iobbi-Nivol, C., J. Pommier, J. Simala-Grant, V. Mejean, and G. Giordano. 1996. High substrate specificity and induction characteristics of trimethylamine-N-oxide reductase of Escherichia coli. Biochim. Biophys. Acta 1294:77-82.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 77-82
    • Iobbi-Nivol, C.1    Pommier, J.2    Simala-Grant, J.3    Mejean, V.4    Giordano, G.5
  • 17
    • 0032835259 scopus 로고    scopus 로고
    • Response of hya expression to external pH in Escherichia coli
    • King, P. W., and A. E. Przyhyla. 1999. Response of hya expression to external pH in Escherichia coli. J. Bacteriol. 181:5250-5256.
    • (1999) J. Bacteriol. , vol.181 , pp. 5250-5256
    • King, P.W.1    Przyhyla, A.E.2
  • 18
    • 1542304722 scopus 로고    scopus 로고
    • Biosynthesis of metal sites
    • Kuchar, J., and R. P. Hausinger. 2004. Biosynthesis of metal sites. Chem. Rev. 104:509-525.
    • (2004) Chem. Rev. , vol.104 , pp. 509-525
    • Kuchar, J.1    Hausinger, R.P.2
  • 19
    • 0037015025 scopus 로고    scopus 로고
    • Identification of the binding sites of regulatory proteins in bacterial genomes
    • Li, H., V. Rhodius, C. Gross, and E. D. Siggia. 2002. Identification of the binding sites of regulatory proteins in bacterial genomes. Proc. Natl. Acad. Sci. USA 99:11772-11777.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11772-11777
    • Li, H.1    Rhodius, V.2    Gross, C.3    Siggia, E.D.4
  • 20
    • 0031963196 scopus 로고    scopus 로고
    • The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli
    • MacLean, M. J., L. S. Ness, G. P. Ferguson, and I. R. Booth. 1998. The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli. Mol. Microbiol. 27:563-571.
    • (1998) Mol. Microbiol. , vol.27 , pp. 563-571
    • MacLean, M.J.1    Ness, L.S.2    Ferguson, G.P.3    Booth, I.R.4
  • 21
    • 0035876430 scopus 로고    scopus 로고
    • Fidelity of metal insertion into hydrogenases
    • Magalon, A., M. Blokesch, E. Zehelein, and A. Bock. 2001. Fidelity of metal insertion into hydrogenases. FEBS Lett. 499:73-76.
    • (2001) FEBS Lett. , vol.499 , pp. 73-76
    • Magalon, A.1    Blokesch, M.2    Zehelein, E.3    Bock, A.4
  • 23
    • 0033918228 scopus 로고    scopus 로고
    • Conservation of DNA regulatory motifs and discovery of new motifs in microbial genomes
    • McGuire, A. M., J. D. Hughes, and G. M. Church. 2000. Conservation of DNA regulatory motifs and discovery of new motifs in microbial genomes. Genome Res. 10:744-757.
    • (2000) Genome Res. , vol.10 , pp. 744-757
    • McGuire, A.M.1    Hughes, J.D.2    Church, G.M.3
  • 24
    • 0027482679 scopus 로고
    • The nik operon of Escheriehia coli encodes a periplasmic binding-protein-dependent transport system for nickel
    • Navarro, C., L. F. Wu, and M. A. Mandrand-Berthelot. 1993. The nik operon of Escheriehia coli encodes a periplasmic binding-protein-dependent transport system for nickel. Mol. Microbiol. 9:1181-1191.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1181-1191
    • Navarro, C.1    Wu, L.F.2    Mandrand-Berthelot, M.A.3
  • 25
    • 0037195612 scopus 로고    scopus 로고
    • Molecular hydrogen as an energy source for Helicobacter pylori
    • Olson, J. W., and R. J. Maier. 2002. Molecular hydrogen as an energy source for Helicobacter pylori. Science 298:1788-1790.
    • (2002) Science , vol.298 , pp. 1788-1790
    • Olson, J.W.1    Maier, R.J.2
  • 26
    • 0035997354 scopus 로고    scopus 로고
    • Great metalloclusters in enzymology
    • Rees, D. C. 2002. Great metalloclusters in enzymology. Annu. Rev. Biochem. 71:221-246.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 221-246
    • Rees, D.C.1
  • 27
    • 0032873183 scopus 로고    scopus 로고
    • Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli
    • Richard, D. J., G. Sawers, F. Sargent, L. McWalter, and D. H. Boxer. 1999. Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli. Microbiology 145:2903-2912.
    • (1999) Microbiology , vol.145 , pp. 2903-2912
    • Richard, D.J.1    Sawers, G.2    Sargent, F.3    McWalter, L.4    Boxer, D.H.5
  • 28
    • 0025930768 scopus 로고
    • Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: Definition of the formate regulon
    • Rossmann, R., G. Sawers, and A. Bock. 1991. Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: definition of the formate regulon. Mol. Microbiol. 5:2807-2814.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2807-2814
    • Rossmann, R.1    Sawers, G.2    Bock, A.3
  • 29
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: Evidence for a third isoenzyme
    • Sawers, R. G., S. P. Ballantine, and D. H. Boxer. 1985. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacteriol. 164:1324-1331.
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 30
    • 0347285390 scopus 로고    scopus 로고
    • Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli
    • Self, W. T., A. Hasona, and K. T. Shanmugam. 2004. Expression and regulation of a silent operon, hyf, coding for hydrogenase 4 isoenzyme in Escherichia coli. J. Bacteriol. 186:580-587.
    • (2004) J. Bacteriol. , vol.186 , pp. 580-587
    • Self, W.T.1    Hasona, A.2    Shanmugam, K.T.3
  • 31
    • 0026059559 scopus 로고
    • Magnesium transport in Salmonella typhimurium. Regulation of mgtA and mgtB expression
    • Snavely, M. D., S. A. Gravina, T. T. Cheung, C. G. Miller, and M. E. Maguire. 1991. Magnesium transport in Salmonella typhimurium. Regulation of mgtA and mgtB expression. J. Biol. Chew. 266:824-829.
    • (1991) J. Biol. Chew. , vol.266 , pp. 824-829
    • Snavely, M.D.1    Gravina, S.A.2    Cheung, T.T.3    Miller, C.G.4    Maguire, M.E.5
  • 32
    • 0015958425 scopus 로고
    • Proteins of the inner membrane of Escherichia coli: Changes in composition associated with anaerobic growth and fumarate reductase amber mutation
    • Spencer, M. E., and J. R. Guest. 1974. Proteins of the inner membrane of Escherichia coli: changes in composition associated with anaerobic growth and fumarate reductase amber mutation. J. Bacteriol. 117:954-959.
    • (1974) J. Bacteriol. , vol.117 , pp. 954-959
    • Spencer, M.E.1    Guest, J.R.2
  • 33
    • 0037326468 scopus 로고    scopus 로고
    • Biochemical Society Special Lecture. Nitrate- and nitrite-responsive sensors NarX and NarQ of proteobacteria
    • Stewart, V. 2003. Biochemical Society Special Lecture. Nitrate- and nitrite-responsive sensors NarX and NarQ of proteobacteria. Biochem. Soc. Trans. 31:1-10.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1-10
    • Stewart, V.1
  • 34
    • 0024094677 scopus 로고
    • Influence ol nar (nitrate reductase) genes on nitrate inhibition of formate-hydrogen lyase and fumarate reductase gene expression in Escherichia coli K-12
    • Stewart, V., and B. L. Berg. 1988. Influence ol nar (nitrate reductase) genes on nitrate inhibition of formate-hydrogen lyase and fumarate reductase gene expression in Escherichia coli K-12. J. Bacteriol. 170:4437-4444.
    • (1988) J. Bacteriol. , vol.170 , pp. 4437-4444
    • Stewart, V.1    Berg, B.L.2
  • 35
    • 9444245016 scopus 로고    scopus 로고
    • Distinct classes of glyoxalase I: Metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes
    • Sukdeo, N., S. L. Clugston, E. Daub, and J. F. Honek. 2004. Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes. Biochem. J. 384:111-117.
    • (2004) Biochem. J. , vol.384 , pp. 111-117
    • Sukdeo, N.1    Clugston, S.L.2    Daub, E.3    Honek, J.F.4
  • 36
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer, R. K. 1998. Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144:2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 37
    • 0028064605 scopus 로고
    • A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach
    • Tsuda, M., M. Karita, M. G. Morshed, K. Okita, and T. Nakazawa. 1994. A urease-negative mutant of Helicobacter pylori constructed by allelic exchange mutagenesis lacks the ability to colonize the nude mouse stomach. Infect. Immun. 62:3586-3589.
    • (1994) Infect. Immun. , vol.62 , pp. 3586-3589
    • Tsuda, M.1    Karita, M.2    Morshed, M.G.3    Okita, K.4    Nakazawa, T.5
  • 38
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden, G., and J. Bongaerts. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta 1320:217-234.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 39
    • 0242695597 scopus 로고    scopus 로고
    • The active site and catalytic mechanism of NiFe hydrogenases
    • Volheda, A., and J. C. Fontecilla-Camps. 2003. The active site and catalytic mechanism of NiFe hydrogenases. Dalton Trans. 2003:4030-4038.
    • (2003) Dalton Trans. , vol.2003 , pp. 4030-4038
    • Volheda, A.1    Fontecilla-Camps, J.C.2
  • 40
    • 0032835980 scopus 로고    scopus 로고
    • The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite
    • Wang, H., C.-P. Tseng, and R. P. Gunsalus. 1999. The napF and narG nitrate reductase operons in Escherichia coli are differentially expressed in response to submicromolar concentrations of nitrate but not nitrite. J. Bacteriol. 181:5303-5308.
    • (1999) J. Bacteriol. , vol.181 , pp. 5303-5308
    • Wang, H.1    Tseng, C.-P.2    Gunsalus, R.P.3
  • 41
    • 3543056937 scopus 로고    scopus 로고
    • Selectivity of metal binding and metal-induced stability of Escherichia coli NikR
    • Wang, S. C., A. V. Dias, S. L. Bloom, and D. B. Zambie. 2004. Selectivity of metal binding and metal-induced stability of Escherichia coli NikR. Biochemistry 43:10018-10028.
    • (2004) Biochemistry , vol.43 , pp. 10018-10028
    • Wang, S.C.1    Dias, A.V.2    Bloom, S.L.3    Zambie, D.B.4
  • 42
    • 0023986420 scopus 로고
    • Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzymc with broad substrate spccificity
    • Weiner, J. H., D. P. MacIsaac, R. E. Bishop, and P. T. Bilous. 1988. Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzymc with broad substrate spccificity. J. Bacteriol. 170:1505-1510.
    • (1988) J. Bacteriol. , vol.170 , pp. 1505-1510
    • Weiner, J.H.1    MacIsaac, D.P.2    Bishop, R.E.3    Bilous, P.T.4
  • 43
    • 0022639247 scopus 로고
    • Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity
    • Wu, L. F., and M. A. Mandrand-Berthelot. 1986. Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity. Biochimie 68:167-179.
    • (1986) Biochimie , vol.68 , pp. 167-179
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 44
    • 0024836127 scopus 로고
    • Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr muuinis in Escherichia coli
    • Wu, L. F., M. A. Mandrand-Berthelot, R. Waugh, C. J. Edmonds, S. E. Holt, and D. H. Boxer. 1989. Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr muuinis in Escherichia coli. Mol. Microbiol. 3:1709-1718.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1709-1718
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2    Waugh, R.3    Edmonds, C.J.4    Holt, S.E.5    Boxer, D.H.6
  • 45
    • 0025984451 scopus 로고
    • The hydC region contains a multi-cistronic operon (nik) involved in nickel transport in Escherichia coli
    • Wu, L. F., C. Navarro, and M. A. Mandrand-Berthelot. 1991. The hydC region contains a multi-cistronic operon (nik) involved in nickel transport in Escherichia coli. Gene 107:37-42.
    • (1991) Gene , vol.107 , pp. 37-42
    • Wu, L.F.1    Navarro, C.2    Mandrand-Berthelot, M.A.3
  • 46
    • 0043032929 scopus 로고    scopus 로고
    • Phenotype microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems
    • Zhou, L., X.-H. Lei, B. R. Bochner, and B. L. Wanner. 2003. Phenotype microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems. J. Bacteriol. 185:4956-4972.
    • (2003) J. Bacteriol. , vol.185 , pp. 4956-4972
    • Zhou, L.1    Lei, X.-H.2    Bochner, B.R.3    Wanner, B.L.4


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