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Volumn 73, Issue 11, 2005, Pages 7252-7258

The nickel-responsive regulator NikR controls activation and repression of gene transcription in Helicobacter pylori

Author keywords

[No Author keywords available]

Indexed keywords

DNA; NICKEL; NIKR PROTEIN; REGULATOR PROTEIN; RNA; UNCLASSIFIED DRUG; UREASE;

EID: 27744569940     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.11.7252-7258.2005     Document Type: Article
Times cited : (90)

References (47)
  • 1
    • 0034076830 scopus 로고    scopus 로고
    • Identification of the urease operon in Helicobacter pylon and its control by mRNA decay in response to pH
    • Akada, J. K., M. Shirai, H. Takeuchi, M. Tsuda, and T. Nakazawa. 2000. Identification of the urease operon in Helicobacter pylon and its control by mRNA decay in response to pH. Mol. Microbiol. 36:1071-1084.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1071-1084
    • Akada, J.K.1    Shirai, M.2    Takeuchi, H.3    Tsuda, M.4    Nakazawa, T.5
  • 3
    • 0031042034 scopus 로고    scopus 로고
    • Synthesis and activity of Helicobacter pylori urease and catalase at low pH
    • Bauerfeind, P., R. Garner, B. E. Dunn, and H. L. Mobley. 1997. Synthesis and activity of Helicobacter pylori urease and catalase at low pH. Gut 40:25-30.
    • (1997) Gut , vol.40 , pp. 25-30
    • Bauerfeind, P.1    Garner, R.2    Dunn, B.E.3    Mobley, H.L.4
  • 4
    • 0029994917 scopus 로고    scopus 로고
    • Allelic exchange mutagenesis of nixA in Helicobacter pylori results in reduced nickel transport and urease activity
    • Bauerfeind, P., R. M. Garner, and L. T. Mobley. 1996. Allelic exchange mutagenesis of nixA in Helicobacter pylori results in reduced nickel transport and urease activity. Infect. Immun. 64:2877-2880.
    • (1996) Infect. Immun. , vol.64 , pp. 2877-2880
    • Bauerfeind, P.1    Garner, R.M.2    Mobley, L.T.3
  • 5
    • 0032882219 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa AlgZ, a ribbon-helix-helix DNA-binding protein, is essential for alginate synthesis and algD transcriptional activation
    • Baynham, P. J., A. L. Brown, L. L. Hall, and D. J. Wozniak. 1999. Pseudomonas aeruginosa AlgZ, a ribbon-helix-helix DNA-binding protein, is essential for alginate synthesis and algD transcriptional activation. Mol. Microbiol. 33:1069-1080.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1069-1080
    • Baynham, P.J.1    Brown, A.L.2    Hall, L.L.3    Wozniak, D.J.4
  • 6
    • 0033759351 scopus 로고    scopus 로고
    • Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacterpylori
    • Bereswill, S., S. Greiner, A. H. van Vliet, B. Waidner, F. Fassbinder, E. Schlitz, J. G. Kusters, and M. Kist. 2000. Regulation of ferritin-mediated cytoplasmic iron storage by the ferric uptake regulator homolog (Fur) of Helicobacterpylori. J. Bacteriol. 182:5948-5953.
    • (2000) J. Bacteriol. , vol.182 , pp. 5948-5953
    • Bereswill, S.1    Greiner, S.2    Van Vliet, A.H.3    Waidner, B.4    Fassbinder, F.5    Schlitz, E.6    Kusters, J.G.7    Kist, M.8
  • 7
    • 0032958594 scopus 로고    scopus 로고
    • Identification of virulence genes of Helicobacter pylori by random insertion mutagenesis
    • Bijisma, J. J., C. M. Vandenbroucke-Grauls, S. H. Phadnis, and J. G. Kusters. 1999. Identification of virulence genes of Helicobacter pylori by random insertion mutagenesis. Infect. Immun. 67:2433-2440.
    • (1999) Infect. Immun. , vol.67 , pp. 2433-2440
    • Bijisma, J.J.1    Vandenbroucke-Grauls, C.M.2    Phadnis, S.H.3    Kusters, J.G.4
  • 8
    • 3543072246 scopus 로고    scopus 로고
    • Metal-selective DNA-binding response of Escherichia coli NikR
    • Bloom, S. L., and D. B. Zamble. 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    Zamble, D.B.2
  • 10
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori
    • Bury-Mone, S., J. M. Thiberge, M. Contreras, A. Maitournam, A. Labigne, and H. De Reuse. 2004. Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori. Mol. Microbiol. 53:623-638.
    • (2004) Mol. Microbiol. , vol.53 , pp. 623-638
    • Bury-Mone, S.1    Thiberge, J.M.2    Contreras, M.3    Maitournam, A.4    Labigne, A.5    De Reuse, H.6
  • 12
    • 0032697047 scopus 로고    scopus 로고
    • NikR is a ribbon-helix-helix DNA-binding protein
    • Chivers, P. T., and R. T. Sauer. 1999. NikR is a ribbon-helix-helix DNA-binding protein. Protein Sci. 8:2494-2500.
    • (1999) Protein Sci. , vol.8 , pp. 2494-2500
    • Chivers, P.T.1    Sauer, R.T.2
  • 13
    • 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
  • 14
    • 0034733505 scopus 로고    scopus 로고
    • 2+-dependent interaction of NikR with wild-type and mutant operator sites
    • 2+-dependent 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
  • 15
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori
    • Contreras, M., J. M. Thiberge, M. A. Mandrand-Berthelot, and A. Labigne. 2003. Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori. Mol. Microbiol. 49:947-963.
    • (2003) Mol. Microbiol. , vol.49 , pp. 947-963
    • Contreras, M.1    Thiberge, J.M.2    Mandrand-Berthelot, M.A.3    Labigne, A.4
  • 16
    • 27744517876 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Birmingham, Birmingham, United Kingdom
    • Davies, B. J. 2001. The expression, regulation and biological importance of the urease enzyme of Helicobacter pylori. Ph.D. thesis. University of Birmingham, Birmingham, United Kingdom.
    • (2001)
    • Davies, B.J.1
  • 18
    • 3042816068 scopus 로고    scopus 로고
    • Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis
    • Delany, I., R. Rappuoli, and V. Scarlato. 2004. Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol. Microbiol. 52:1081-1090.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1081-1090
    • Delany, I.1    Rappuoli, R.2    Scarlato, V.3
  • 19
    • 0035724513 scopus 로고    scopus 로고
    • The fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori
    • Delany, I., G. Spohn, R. Rappuoli, and V. Scarlato. 2001. The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori. Mol. Microbiol. 42:1297-1309.
    • (2001) Mol. Microbiol. , vol.42 , pp. 1297-1309
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 20
    • 0032932493 scopus 로고    scopus 로고
    • Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli
    • De Pina, K., V. Desjardin, M. A. Mandrand-Berthelot, G. Giordano, and L. F. Wu. 1999. Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli. J. Bacteriol. 181:670-674.
    • (1999) J. Bacteriol. , vol.181 , pp. 670-674
    • De Pina, K.1    Desjardin, V.2    Mandrand-Berthelot, M.A.3    Giordano, G.4    Wu, L.F.5
  • 24
    • 0031982679 scopus 로고    scopus 로고
    • Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions
    • Fulkerson, J. F., Jr., R. M. Garner, and H. L. Mobley. 1998. Conserved residues and motifs in the NixA protein of Helicobacter pylori are critical for the high affinity transport of nickel ions. J. Biol. Chem. 273:235-241.
    • (1998) J. Biol. Chem. , vol.273 , pp. 235-241
    • Fulkerson Jr., J.F.1    Garner, R.M.2    Mobley, H.L.3
  • 25
    • 0034104188 scopus 로고    scopus 로고
    • Membrane topology of the NixA nickel transporter of Helicobacter pylori: Two nickel transport-specific motifs within transmembrane helices II and III
    • Fulkerson, J. F., Jr., and H. L. Mobley. 2000. Membrane topology of the NixA nickel transporter of Helicobacter pylori: two nickel transport-specific motifs within transmembrane helices II and III. J. Bacteriol. 182:1722-1730.
    • (2000) J. Bacteriol. , vol.182 , pp. 1722-1730
    • Fulkerson Jr., J.F.1    Mobley, H.L.2
  • 26
    • 0035169902 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages
    • Gold, B., G. M. Rodriguez, S. A. Marras, M. Pentecost, and I. Smith. 2001. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol. Microbiol. 42:851-865.
    • (2001) Mol. Microbiol. , vol.42 , pp. 851-865
    • Gold, B.1    Rodriguez, G.M.2    Marras, S.A.3    Pentecost, M.4    Smith, I.5
  • 27
    • 0033192731 scopus 로고    scopus 로고
    • Role of Hpn and NixA of Helicobacter pylori in susceptibility and resistance to bismuth and other metal ions
    • Mobley, H. L., R. M. Garner, G. R. Chippendale, J. V. Gilbert, A. V. Kane, and A. G. Plaut. 1999. Role of Hpn and NixA of Helicobacter pylori in susceptibility and resistance to bismuth and other metal ions. Helicobacter 4:162-169.
    • (1999) Helicobacter , vol.4 , pp. 162-169
    • Mobley, H.L.1    Garner, R.M.2    Chippendale, G.R.3    Gilbert, J.V.4    Kane, A.V.5    Plaut, A.G.6
  • 28
    • 0038203196 scopus 로고    scopus 로고
    • Nickel uptake and utilization by microorganisms
    • Mulrooney, S. B., and R. P. Hausinger. 2003. Nickel uptake and utilization by microorganisms. FEMS Microbiol. Rev. 27:239-261.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 239-261
    • Mulrooney, S.B.1    Hausinger, R.P.2
  • 30
    • 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
  • 31
    • 21144455097 scopus 로고    scopus 로고
    • Binding of Pseudomonas aeruginosa AlgZ to sites upstream of the algZ promoter leads to repression of transcription
    • Ramsey, D. M., P. J. Baynham, and D. J. Wozniak. 2005. Binding of Pseudomonas aeruginosa AlgZ to sites upstream of the algZ promoter leads to repression of transcription. J. Bacteriol. 187:4430-4443.
    • (2005) J. Bacteriol. , vol.187 , pp. 4430-4443
    • Ramsey, D.M.1    Baynham, P.J.2    Wozniak, D.J.3
  • 32
    • 0028177303 scopus 로고
    • DNA recognition by β-sheets in the Arc repressor-operator crystal structure
    • Raumann, B. E., M. A. Rould, C. O. Pabo, and R. T. Sauer. 1994. DNA recognition by β-sheets in the Arc repressor-operator crystal structure. Nature 367:754-757.
    • (1994) Nature , vol.367 , pp. 754-757
    • Raumann, B.E.1    Rould, M.A.2    Pabo, C.O.3    Sauer, R.T.4
  • 33
    • 0037344575 scopus 로고    scopus 로고
    • Mechanisms of iron regulation in mycobacteria: Role in physiology and virulence
    • Rodriguez, G. M., and I. Smith. 2003. Mechanisms of iron regulation in mycobacteria: role in physiology and virulence. Mol. Microbiol. 47:1485-1494.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1485-1494
    • Rodriguez, G.M.1    Smith, I.2
  • 36
    • 0032757429 scopus 로고    scopus 로고
    • Activation of Helicobacter pylori ureA promoter by a hybrid Escherichia coli-H. pylori rpoD gene in E. coli
    • Shirai, M., R. Fujinaga, J. K. Akada, and T. Nakazawa. 1999. Activation of Helicobacter pylori ureA promoter by a hybrid Escherichia coli-H. pylori rpoD gene in E. coli. Gene 239:351-359.
    • (1999) Gene , vol.239 , pp. 351-359
    • Shirai, M.1    Fujinaga, R.2    Akada, J.K.3    Nakazawa, T.4
  • 37
    • 0029786848 scopus 로고    scopus 로고
    • Dual regulation of open-complex formation and promoter clearance by Arc explains a novel repressor to activator switch
    • Smith, T. L., and R. T. Sauer. 1996. Dual regulation of open-complex formation and promoter clearance by Arc explains a novel repressor to activator switch. Proc. Natl. Acad. Sci. USA 93:8868-8872.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8868-8872
    • Smith, T.L.1    Sauer, R.T.2
  • 39
    • 5644252852 scopus 로고    scopus 로고
    • NikR-mediated regulation of Helicobacter pylori acid adaptation
    • van Vliet, A. H. M., F. D. Ernst, and J. G. Kusters. 2004. NikR-mediated regulation of Helicobacter pylori acid adaptation. Trends Microbiol. 12:489-494.
    • (2004) Trends Microbiol. , vol.12 , pp. 489-494
    • Van Vliet, A.H.M.1    Ernst, F.D.2    Kusters, J.G.3
  • 40
    • 0842305636 scopus 로고    scopus 로고
    • Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive repressor cascade
    • van Vliet, A. H. M., E. J. Kuipers, J. Stoof, S. W. Poppelaars, and J. G. Kusters. 2004. Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive repressor cascade. Infect. Immun. 72:766-773.
    • (2004) Infect. Immun. , vol.72 , pp. 766-773
    • Van Vliet, A.H.M.1    Kuipers, E.J.2    Stoof, J.3    Poppelaars, S.W.4    Kusters, J.G.5
  • 43
  • 44
    • 0031690670 scopus 로고    scopus 로고
    • Iron-responsive gene regulation in a Campylobacter jejuni for mutant
    • van Vliet, A. H. M., K. G. Wooldridge, and J. M. Ketley. 1998. Iron-responsive gene regulation in a Campylobacter jejuni for mutant. J. Bacteriol. 180:5291-5298.
    • (1998) J. Bacteriol. , vol.180 , pp. 5291-5298
    • Van Vliet, A.H.M.1    Wooldridge, K.G.2    Ketley, J.M.3
  • 46
    • 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. Zamble. 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    Zamble, D.B.4
  • 47
    • 0036175155 scopus 로고    scopus 로고
    • Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobader pylori
    • Wolfram, L., and P. Bauerfeind. 2002. Conserved low-affinity nickel-binding amino acids are essential for the function of the nickel permease NixA of Helicobader pylori. J. Bacteriol. 184:1438-1443.
    • (2002) J. Bacteriol. , vol.184 , pp. 1438-1443
    • Wolfram, L.1    Bauerfeind, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.