메뉴 건너뛰기




Volumn 193, Issue 5, 2011, Pages 1131-1141

In vivo recognition of the fecA3 target promoter by Helicobacter pylori NikR

Author keywords

[No Author keywords available]

Indexed keywords

HPNIKR PROTEIN; HYDROXYL RADICAL; NUCLEOTIDE; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 79951641387     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01153-10     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 33646138246 scopus 로고    scopus 로고
    • The metal- and DNA-binding activities of Helicobacter pylori NikR
    • Abraham, L. O., Y. Li, and D. B. Zamble. 2006. The metal- and DNA-binding activities of Helicobacter pylori NikR. J. Inorg. Biochem. 100:1005-1014.
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 1005-1014
    • Abraham, L.O.1    Li, Y.2    Zamble, D.B.3
  • 2
    • 77953257812 scopus 로고    scopus 로고
    • Structural and mechanistic insights into Helicobacter pylori NikR activation
    • Bahlawane, C., et al. 2010. Structural and mechanistic insights into Helicobacter pylori NikR activation. Nucleic Acids Res. 38:3106-3118.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3106-3118
    • Bahlawane, C.1
  • 3
    • 0031696507 scopus 로고    scopus 로고
    • Functional analysis of the Helicobacter pylori principal sigma subunit of RNA polymerase reveals that the spacer region is important for efficient transcription
    • Beier, D., G. Spohn, R. Rappuoli, and V. Scarlato. 1998. Functional analysis of the Helicobacter pylori principal sigma subunit of RNA polymerase reveals that the spacer region is important for efficient transcription. Mol. Microbiol. 30:121-134.
    • (1998) Mol. Microbiol. , vol.30 , pp. 121-134
    • Beier, D.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 4
    • 64049107915 scopus 로고    scopus 로고
    • An intact urease assembly pathway is required to compete with NikR for nickel ions in Helicobacter pylori
    • Benanti, E. L., and P. T. Chivers. 2009. An intact urease assembly pathway is required to compete with NikR for nickel ions in Helicobacter pylori. J. Bacteriol. 191:2405-2408.
    • (2009) J. Bacteriol. , vol.191 , pp. 2405-2408
    • Benanti, E.L.1    Chivers, P.T.2
  • 5
    • 34547130605 scopus 로고    scopus 로고
    • The N-terminal arm of the Helicobacter pylori Ni2+-dependent transcription factor NikR is required for specific DNA binding
    • Benanti, E. L., and P. T. Chivers. 2007. The N-terminal arm of the Helicobacter pylori Ni2+-dependent transcription factor NikR is required for specific DNA binding. J. Biol. Chem. 282:20365-20375.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20365-20375
    • Benanti, E.L.1    Chivers, P.T.2
  • 6
    • 1842591130 scopus 로고    scopus 로고
    • The regulation of bacterial transcription initiation
    • Browning, D. F., and S. J. Busby. 2004. The regulation of bacterial transcription initiation. Nat. Rev. Microbiol. 2:57-65.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 57-65
    • Browning, D.F.1    Busby, S.J.2
  • 7
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to activity via metal ion regulators mediates virulense in the gastric pathogen Helicobacter pylori
    • DOI 10.1111/j.1365-2958.2004.04137.x
    • Bury-Mone, S., et al. 2004. Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori. Mol. Microbiol. 53:623-638. (Pubitemid 38998180)
    • (2004) Molecular Microbiology , vol.53 , Issue.2 , pp. 623-638
    • Bury-Mone, S.1    Thiberge, J.-M.2    Contreras, M.3    Maitournam, A.4    Labigne, A.5    De, R.H.6
  • 8
    • 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
  • 9
    • 0034733505 scopus 로고    scopus 로고
    • Regulation of high affinity nickel uptake in bacteria. Ni2+-dependent 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+-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
  • 10
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori
    • DOI 10.1046/j.1365-2958.2003.03621.x
    • 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. (Pubitemid 36981341)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 947-963
    • Contreras, M.1    Thiberge, J.-M.2    Mandrand-Berthelot, M.-A.3    Labigne, A.4
  • 11
    • 0035816213 scopus 로고    scopus 로고
    • Plasmid transcriptional repressor CopG oligomerises to render helical superstructures unbound and in complexes with oligonucleotides
    • Costa, M., et al. 2001. Plasmid transcriptional repressor CopG oligomerises to render helical superstructures unbound and in complexes with oligonucleotides. J. Mol. Biol. 310:403-417.
    • (2001) J. Mol. Biol. , vol.310 , pp. 403-417
    • Costa, M.1
  • 12
    • 66149112914 scopus 로고    scopus 로고
    • Growth phase and metal-dependent transcriptional regulation of the fecA genes in Helicobacter pylori
    • Danielli, A., et al. 2009. Growth phase and metal-dependent transcriptional regulation of the fecA genes in Helicobacter pylori. J. Bacteriol. 191:3717-3725.
    • (2009) J. Bacteriol. , vol.191 , pp. 3717-3725
    • Danielli, A.1
  • 13
    • 77955129867 scopus 로고    scopus 로고
    • Regulatory circuits in Helicobacter pylori: Network motifs and regulators involved in metal-dependent responses
    • Danielli, A., and V. Scarlato. 2010. Regulatory circuits in Helicobacter pylori: network motifs and regulators involved in metal-dependent responses. FEMS Microbiol. Rev. 34:738-752.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 738-752
    • Danielli, A.1    Scarlato, V.2
  • 14
    • 33845505250 scopus 로고    scopus 로고
    • Helicobacter pylori HP1512 is a nickel-responsive NikR-regulated outer membrane protein
    • Davis, G. S., E. L. Flannery, and H. L. Mobley. 2006. Helicobacter pylori HP1512 is a nickel-responsive NikR-regulated outer membrane protein. Infect. Immun. 74:6811-6820.
    • (2006) Infect. Immun. , vol.74 , pp. 6811-6820
    • Davis, G.S.1    Flannery, E.L.2    Mobley, H.L.3
  • 15
    • 27744481253 scopus 로고    scopus 로고
    • In vitro analysis of protein-operator interactions of the NikR and fur metal-responsive regulators of coregulated genes in Helicobacter pylori
    • DOI 10.1128/JB.187.22.7703-7715.2005
    • Delany, I., et al. 2005. In vitro analysis of protein-operator interactions of the NikR and fur metal-responsive regulators of coregulated genes in Helicobacter pylori. J. Bacteriol. 187:7703-7715. (Pubitemid 41587709)
    • (2005) Journal of Bacteriology , vol.187 , Issue.22 , pp. 7703-7715
    • Delany, I.1    Ieva, R.2    Soragni, A.3    Hilleringmann, M.4    Rappuoli, R.5    Scarlato, V.6
  • 16
    • 0036718563 scopus 로고    scopus 로고
    • Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori
    • Delany, I., G. Spohn, R. Rappuoli, and V. Scarlato. 2002. Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori. J. Bacteriol. 184:4800-4810.
    • (2002) J. Bacteriol. , vol.184 , pp. 4800-4810
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 17
    • 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
  • 18
    • 33746849786 scopus 로고    scopus 로고
    • Structural basis of the nickel response in Helicobacter pylori: Crystal structures of HpNikR in apo and nickel-bound states
    • Dian, C., et al. 2006. Structural basis of the nickel response in Helicobacter pylori: crystal structures of HpNikR in apo and nickel-bound states. J. Mol. Biol. 361:715-730.
    • (2006) J. Mol. Biol. , vol.361 , pp. 715-730
    • Dian, C.1
  • 19
    • 33847646219 scopus 로고    scopus 로고
    • Characterization of the Helicobacter pylori NikR-P(ureA) DNA interaction: Metal ion requirements and sequence specificity
    • Dosanjh, N. S., N. A. Hammerbacher, and S. L. Michel. 2007. Characterization of the Helicobacter pylori NikR-P(ureA) DNA interaction: metal ion requirements and sequence specificity. Biochemistry 46:2520-2529.
    • (2007) Biochemistry , vol.46 , pp. 2520-2529
    • Dosanjh, N.S.1    Hammerbacher, N.A.2    Michel, S.L.3
  • 20
    • 59249087478 scopus 로고    scopus 로고
    • Helicobacter pylori NikR's interaction with DNA: A two-tiered mode of recognition
    • Dosanjh, N. S., A. L. West, and S. L. Michel. 2009. Helicobacter pylori NikR's interaction with DNA: a two-tiered mode of recognition. Biochemistry 48:527-536.
    • (2009) Biochemistry , vol.48 , pp. 527-536
    • Dosanjh, N.S.1    West, A.L.2    Michel, S.L.3
  • 22
    • 33845488317 scopus 로고    scopus 로고
    • NikR mediates nickel-responsive transcriptional repression of the Helicobacter pylori outer membrane proteins FecA3 (HP1400) and FrpB4 (HP1512)
    • Ernst, F. D., et al. 2006. NikR mediates nickel-responsive transcriptional repression of the Helicobacter pylori outer membrane proteins FecA3 (HP1400) and FrpB4 (HP1512). Infect. Immun. 74:6821-6828.
    • (2006) Infect. Immun. , vol.74 , pp. 6821-6828
    • Ernst, F.D.1
  • 23
    • 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
  • 24
    • 64849097266 scopus 로고    scopus 로고
    • The pH-responsive DNA-binding activity of Helicobacter pylori NikR
    • Li, Y., and D. Zamble. 2009. The pH-responsive DNA-binding activity of Helicobacter pylori NikR. Biochemistry 48:2486-2496.
    • (2009) Biochemistry , vol.48 , pp. 2486-2496
    • Li, Y.1    Zamble, D.2
  • 25
    • 0031974434 scopus 로고    scopus 로고
    • Three-minute G + A specific reaction for DNA sequencing
    • Liu, S. T., and G. F. Hong. 1998. Three-minute G + A specific reaction for DNA sequencing. Anal. Biochem. 255:158-159.
    • (1998) Anal. Biochem. , vol.255 , pp. 158-159
    • Liu, S.T.1    Hong, G.F.2
  • 26
    • 73349109189 scopus 로고    scopus 로고
    • The Staphylococcus aureus pSK41 plasmid-encoded ArtA protein is a master regulator of plasmid transmission genes and contains a RHH motif used in alternate DNA-binding modes
    • Ni, L., et al. 2009. The Staphylococcus aureus pSK41 plasmid-encoded ArtA protein is a master regulator of plasmid transmission genes and contains a RHH motif used in alternate DNA-binding modes. Nucleic Acids Res. 37:6970-6983.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6970-6983
    • Ni, L.1
  • 27
    • 70350552019 scopus 로고    scopus 로고
    • RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB
    • Overgaard, M., J. Borch, and K. Gerdes. 2009. RelB and RelE of Escherichia coli form a tight complex that represses transcription via the ribbon-helix-helix motif in RelB. J. Mol. Biol. 394:183-196.
    • (2009) J. Mol. Biol. , vol.394 , pp. 183-196
    • Overgaard, M.1    Borch, J.2    Gerdes, K.3
  • 28
    • 0030798605 scopus 로고    scopus 로고
    • Clues and consequences of DNA bending in transcription
    • Perez-Martin, J., and V. de Lorenzo. 1997. Clues and consequences of DNA bending in transcription. Annu. Rev. Microbiol. 51:593-628.
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 593-628
    • Perez-Martin, J.1    De Lorenzo, V.2
  • 29
    • 25444522923 scopus 로고    scopus 로고
    • Acid-induced activation of the urease promoters is mediated directly by the ArsRS two-component system of Helicobacter pylori
    • DOI 10.1128/IAI.73.10.6437-6445.2005
    • Pflock, M., S. Kennard, I. Delany, V. Scarlato, and D. Beier. 2005. Acid-induced activation of the urease promoters is mediated directly by the ArsRS two-component system of Helicobacter pylori. Infect. Immun. 73:6437-6445. (Pubitemid 41368805)
    • (2005) Infection and Immunity , vol.73 , Issue.10 , pp. 6437-6445
    • Pflock, M.1    Kennard, S.2    Delany, I.3    Scarlato, V.4    Beier, D.5
  • 30
    • 70350686719 scopus 로고    scopus 로고
    • The role of DNA shape in protein-DNA recognition
    • Rohs, R., W. S. M. A. Sosinsky, P. Liu, R. S. Mann, and B. Honig. 2009. The role of DNA shape in protein-DNA recognition. Nature 461:1248-1254.
    • (2009) Nature , vol.461 , pp. 1248-1254
    • Rohs, R.1    Sosinsky, W.S.M.A.2    Liu, P.3    Mann, R.S.4    Honig, B.5
  • 33
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: Variations on a theme
    • Schreiter, E. R., and C. L. Drennan. 2007. Ribbon-helix-helix transcription factors: variations on a theme. Nat. Rev. Microbiol. 5:710-720.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 710-720
    • Schreiter, E.R.1    Drennan, C.L.2
  • 34
    • 0141841775 scopus 로고    scopus 로고
    • Crystal structure of the nickel-responsive transcription factor NikR
    • Schreiter, E. R., et al. 2003. Crystal structure of the nickel-responsive transcription factor NikR. Nat. Struct. Biol. 10:794-799.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 794-799
    • Schreiter, E.R.1
  • 35
    • 33748773334 scopus 로고    scopus 로고
    • NikR-operator complex structure and the mechanism of repressor activation by metal ions
    • Schreiter, E. R., S. C. Wang, D. B. Zamble, and C. L. Drennan. 2006. NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proc. Natl. Acad. Sci. U. S. A. 103:13676-13681.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13676-13681
    • Schreiter, E.R.1    Wang, S.C.2    Zamble, D.B.3    Drennan, C.L.4
  • 36
    • 0030728522 scopus 로고    scopus 로고
    • Transcriptional analysis of the divergent cagAB genes encoded by the pathogenicity island of Helicobacter pylori
    • Spohn, G., D. Beier, R. Rappuoli, and V. Scarlato. 1997. Transcriptional analysis of the divergent cagAB genes encoded by the pathogenicity island of Helicobacter pylori. Mol. Microbiol. 26:361-372. (Pubitemid 27483684)
    • (1997) Molecular Microbiology , vol.26 , Issue.2 , pp. 361-372
    • Spohn, G.1    Beier, D.2    Rappuoli, R.3    Scarlato, V.4
  • 37
    • 77949424577 scopus 로고    scopus 로고
    • Characterization of NikR-responsive promoters of urease and metal transport genes of Helicobacter mustelae
    • Stoof, J., E. J. Kuipers, and A. H. van Vliet. 2010. Characterization of NikR-responsive promoters of urease and metal transport genes of Helicobacter mustelae. Biometals 23:145-159.
    • (2010) Biometals , vol.23 , pp. 145-159
    • Stoof, J.1    Kuipers, E.J.2    Van Vliet, A.H.3
  • 38
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 39
    • 5644252852 scopus 로고    scopus 로고
    • NikR-mediated regulation of Helicobacter pylori acid adaptation
    • van Vliet, A. H., 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.1    Ernst, F.D.2    Kusters, J.G.3
  • 40
    • 0036263248 scopus 로고    scopus 로고
    • NikR mediates nickel-responsive transcriptional induction of urease expression in Helicobacter pylori
    • van Vliet, A. H., et al. 2002. NikR mediates nickel-responsive transcriptional induction of urease expression in Helicobacter pylori. Infect. Immun. 70:2846-2852.
    • (2002) Infect. Immun. , vol.70 , pp. 2846-2852
    • Van Vliet, A.H.1
  • 41
    • 0025132642 scopus 로고
    • Chloramphenicol resistance in Campylobacter coli: Nucleotide sequence, expression, and cloning vector construction
    • Wang, Y., and D. E. Taylor. 1990. Chloramphenicol resistance in Campylobacter coli: nucleotide sequence, expression, and cloning vector construction. Gene 94:23-28.
    • (1990) Gene , vol.94 , pp. 23-28
    • Wang, Y.1    Taylor, D.E.2
  • 42
    • 77958063110 scopus 로고    scopus 로고
    • Holo-Ni(II) HpNikR is an asymmetric tetramer containing two different nickel-binding sites
    • West, A. L., et al. 2010. Holo-Ni(II) HpNikR is an asymmetric tetramer containing two different nickel-binding sites. J. Am. Chem. Soc. 132:14447-14456.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14447-14456
    • West, A.L.1
  • 43
    • 32444446916 scopus 로고    scopus 로고
    • Nickel represses the synthesis of the nickel permease NixA of Helicobacter pylori
    • DOI 10.1128/JB.188.4.1245-1250.2006
    • Wolfram, L., E. Haas, and P. Bauerfeind. 2006. Nickel represses the synthesis of the nickel permease NixA of Helicobacter pylori. J. Bacteriol. 188:1245-1250. (Pubitemid 43228656)
    • (2006) Journal of Bacteriology , vol.188 , Issue.4 , pp. 1245-1250
    • Wolfram, L.1    Haas, E.2    Bauerfeind, P.3
  • 44
    • 0028860071 scopus 로고
    • Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin
    • Xiang, Z., et al. 1995. Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vacuolating cytotoxin. Infect. Immun. 63:94-98.
    • (1995) Infect. Immun. , vol.63 , pp. 94-98
    • Xiang, Z.1
  • 45
    • 53549085686 scopus 로고    scopus 로고
    • High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter
    • Zambelli, B., et al. 2008. High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter. J. Mol. Biol. 383:1129-1143.
    • (2008) J. Mol. Biol. , vol.383 , pp. 1129-1143
    • Zambelli, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.