메뉴 건너뛰기




Volumn 38, Issue 9, 2010, Pages 3106-3118

Structural and mechanistic insights into Helicobacter pylori NikR activation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MUTANT PROTEIN; NICKEL; PROTEIN NIKR; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; NIKR PROTEIN, HELICOBACTER PYLORI; REPRESSOR PROTEIN;

EID: 77953257812     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1216     Document Type: Article
Times cited : (34)

References (45)
  • 1
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron, K.J. and Robinson, N.J. (2009) How do bacterial cells ensure that metalloproteins get the correct metal? Nat. Rev. Microbiol., 7, 25-35.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 2
    • 33645228520 scopus 로고    scopus 로고
    • Microbial nickel metalloregulation: NikRs for nickel ions
    • Dosanjh, N.S. and Michel, S.L. (2006) Microbial nickel metalloregulation: NikRs for nickel ions. Curr. Opin. Chem. Biol., 10, 123-130.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 123-130
    • Dosanjh, N.S.1    Michel, S.L.2
  • 3
    • 0032932493 scopus 로고    scopus 로고
    • Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli
    • De Pina, K., Desjardin, V., Mandrand-Berthelot, M.A., Giordano, G. and Wu, L.F. (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
  • 4
    • 33846948997 scopus 로고    scopus 로고
    • Bacterial factors that mediate colonization of the stomach and virulence of Helicobacter pylori
    • Clyne, M., Dolan, B. and Reeves, E.P. (2007) Bacterial factors that mediate colonization of the stomach and virulence of Helicobacter pylori. FEMS Microbiol. Lett., 268, 135-143.
    • (2007) FEMS Microbiol. Lett. , vol.268 , pp. 135-143
    • Clyne, M.1    Dolan, B.2    Reeves, E.P.3
  • 5
    • 34250354686 scopus 로고    scopus 로고
    • Ten years after the first Helicobacter pylori genome: comparative and functional genomics provide new insights in the variability and adaptability of a persistent pathogen
    • de Reuse, H. and Bereswill, S. (2007) Ten years after the first Helicobacter pylori genome: comparative and functional genomics provide new insights in the variability and adaptability of a persistent pathogen. FEMS Immunol. Med. Microbiol., 50, 165-176.
    • (2007) FEMS Immunol. Med. Microbiol. , vol.50 , pp. 165-176
    • de Reuse, H.1    Bereswill, S.2
  • 7
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickel-responsive pleiotropic autoregulator of Helicobacter pylori
    • Contreras, M., Thiberge, J.M., Mandrand-Berthelot, M.A. and Labigne, A. (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
  • 8
    • 27744569940 scopus 로고    scopus 로고
    • The nickel-responsive regulator NikR controls activation and repression of gene transcription in Helicobacter pylori
    • Ernst, F.D., Kuipers, E.J., Heijens, A., Sarwari, R., Stoof, J., Penn, C.W., Kusters, J.G. and van Vliet, A.H. (2005) The nickel-responsive regulator NikR controls activation and repression of gene transcription in Helicobacter pylori. Infect. Immun., 73, 7252-7258.
    • (2005) Infect. Immun. , vol.73 , pp. 7252-7258
    • Ernst, F.D.1    Kuipers, E.J.2    Heijens, A.3    Sarwari, R.4    Stoof, J.5    Penn, C.W.6    Kusters, J.G.7    van Vliet, A.H.8
  • 9
    • 5644252852 scopus 로고    scopus 로고
    • NikR-mediated regulation of Helicobacter pylori acid adaptation
    • van Vliet, A.H., Ernst, F.D. and Kusters, J.G. (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
  • 10
    • 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
    • Delany, I., Ieva, R., Soragni, A., Hilleringmann, M., Rappuoli, R. and Scarlato, V. (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.
    • (2005) J. Bacteriol. , vol.187 , pp. 7703-7715
    • Delany, I.1    Ieva, R.2    Soragni, A.3    Hilleringmann, M.4    Rappuoli, R.5    Scarlato, V.6
  • 11
    • 59249087478 scopus 로고    scopus 로고
    • Helicobacter pylori NikR's interaction with DNA: a two-tiered mode of recognition
    • Dosanjh, N.S., West, A.L. and Michel, S.L.J. (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.J.3
  • 12
    • 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., Stoof, J., Horrevoets, W.M., Kuipers, E.J., Kusters, J.G. and van Vliet, A.H. (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    Stoof, J.2    Horrevoets, W.M.3    Kuipers, E.J.4    Kusters, J.G.5    van Vliet, A.H.6
  • 13
    • 53549085686 scopus 로고    scopus 로고
    • High-affinity Ni2+ binding selectively promotes binding of Helicobacter pylori NikR to its target urease promoter
    • Zambelli, B., Danielli, A., Romagnoli, S., Neyroz, P., Ciurli, S. and Scarlato, V. (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    Danielli, A.2    Romagnoli, S.3    Neyroz, P.4    Ciurli, S.5    Scarlato, V.6
  • 14
    • 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., Schauer, K., Kapp, U., McSweeney, S.M., Labigne, A. and Terradot, L. (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    Schauer, K.2    Kapp, U.3    McSweeney, S.M.4    Labigne, A.5    Terradot, L.6
  • 16
    • 17144395996 scopus 로고    scopus 로고
    • Structure of Pyrococcus horikoshii NikR: nickel sensing and implications for the regulation of DNA recognition
    • Chivers, P.T. and Tahirov, T.H. (2005) Structure of Pyrococcus horikoshii NikR: nickel sensing and implications for the regulation of DNA recognition. J. Mol. Biol., 348, 597-607.
    • (2005) J. Mol. Biol. , vol.348 , pp. 597-607
    • Chivers, P.T.1    Tahirov, T.H.2
  • 17
    • 33748773334 scopus 로고    scopus 로고
    • NikR-operator complex structure and the mechanism of repressor activation by metal ions
    • Schreiter, E.R., Wang, S.C., Zamble, D.B. and Drennan, C.L. (2006) NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proc. Natl Acad. Sci. USA, 103, 13676-13681.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 13676-13681
    • Schreiter, E.R.1    Wang, S.C.2    Zamble, D.B.3    Drennan, C.L.4
  • 18
    • 33646138246 scopus 로고    scopus 로고
    • The metal- and DNA-binding activities of Helicobacter pylori NikR
    • Abraham, L.O., Li, Y. and Zamble, D.B. (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
  • 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., Hammerbacher, N.A. and Michel, S.L. (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
    • 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 Sauer, R.T. (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
  • 22
    • 3543056937 scopus 로고    scopus 로고
    • Selectivity of metal binding and metal-induced stability of Escherichia coli NikR
    • Wang, S.C., Dias, A.V., Bloom, S.L. and Zamble, D.B. (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
  • 24
    • 3543072246 scopus 로고    scopus 로고
    • Metal-selective DNA-binding response of Escherichia coli NikR
    • Bloom, S.L. and Zamble, D.B. (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
  • 25
    • 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 Sauer, R.T. (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
  • 27
    • 67651226891 scopus 로고    scopus 로고
    • Physical basis of metal-binding specificity in Escherichia coli NikR
    • Phillips, C.M., Nerenberg, P.S., Drennan, C.L. and Stultz, C.M. (2009) Physical basis of metal-binding specificity in Escherichia coli NikR. J. Am. Chem. Soc., 131, 10220-10228.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10220-10228
    • Phillips, C.M.1    Nerenberg, P.S.2    Drennan, C.L.3    Stultz, C.M.4
  • 28
    • 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 Chivers, P.T. (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
  • 29
    • 64849097266 scopus 로고    scopus 로고
    • The pH-responsive DNA-binding activity of Helicobacter pylori NikR
    • Li, Y. and Zamble, D. (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
  • 30
    • 66149112914 scopus 로고    scopus 로고
    • Growth phase and metal-dependent transcriptional regulation of the fecA genes in Helicobacter pylori
    • Danielli, A., Romagnoli, S., Roncarati, D., Costantino, L., Delany, I. and Scarlato, V. (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    Romagnoli, S.2    Roncarati, D.3    Costantino, L.4    Delany, I.5    Scarlato, V.6
  • 33
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr., 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 36
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr., 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 38
    • 0031911053 scopus 로고    scopus 로고
    • Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
    • Vanet, A. and Labigne, A. (1998) Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins. Infect. Immun., 66, 1023-1027.
    • (1998) Infect. Immun. , vol.66 , pp. 1023-1027
    • Vanet, A.1    Labigne, A.2
  • 40
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D., Barberato, C. and Koch, M.H.J. (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 42
    • 42649130377 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways
    • Bradley, M.J., Chivers, P.T. and Baker, N.A. (2008) Molecular dynamics simulation of the Escherichia coli NikR protein: equilibrium conformational fluctuations reveal interdomain allosteric communication pathways. J. Mol. Biol., 378, 1155-1173.
    • (2008) J. Mol. Biol. , vol.378 , pp. 1155-1173
    • Bradley, M.J.1    Chivers, P.T.2    Baker, N.A.3
  • 43
    • 33845944628 scopus 로고    scopus 로고
    • The ACT domain: a small molecule binding domain and its role as a common regulatory element
    • Grant, G.A. (2006) The ACT domain: a small molecule binding domain and its role as a common regulatory element. J. Biol. Chem., 281, 33825-33829.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33825-33829
    • Grant, G.A.1
  • 44
    • 66349125424 scopus 로고    scopus 로고
    • The "metallo-specific" response of proteins: a perspective based on the Escherichia coli transcriptional regulator NikR
    • Wang, S.C., Dias, A.V. and Zamble, D.B. (2009) The "metallo-specific" response of proteins: a perspective based on the Escherichia coli transcriptional regulator NikR. Dalton Trans., 2459-2466.
    • (2009) Dalton Trans. , pp. 2459-2466
    • Wang, S.C.1    Dias, A.V.2    Zamble, D.B.3
  • 45
    • 0027741075 scopus 로고
    • Biological monitoring of nickel in humans
    • Sunderman, F.W. Jr (1993) Biological monitoring of nickel in humans. Scand. J. Work Environ. Health, 19(Suppl. 1), 34-38.
    • (1993) Scand. J. Work Environ. Health , vol.19 , Issue.SUPPL. 1 , pp. 34-38
    • Sunderman F.W., Jr.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.