메뉴 건너뛰기




Volumn 48, Issue 11, 2009, Pages 2486-2496

pH-responsive DNA-binding activity of helicobacter pylori NikR

Author keywords

[No Author keywords available]

Indexed keywords

ACID ADAPTATIONS; ACIDIC CONDITIONS; COMPLEX FORMATIONS; DNA BINDINGS; HELICOBACTER PYLORUS; INFLUENCE OF PH; INTERNAL PH; PH-RESPONSIVE; POTENTIAL MECHANISMS; PROMOTER SEQUENCES; QUATERNARY STRUCTURES; SITE-DIRECTED MUTAGENESIS;

EID: 64849097266     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801742r     Document Type: Article
Times cited : (31)

References (64)
  • 1
    • 0035042448 scopus 로고    scopus 로고
    • Helicobacter pylori: Current chemotherapy and new targets for drug design
    • Williamson, J. S. (2001) Helicobacter pylori: current chemotherapy and new targets for drug design. Curr. Pharm. Des. 7, 355-392.
    • (2001) Curr. Pharm. Des , vol.7 , pp. 355-392
    • Williamson, J.S.1
  • 3
    • 0036468233 scopus 로고    scopus 로고
    • Acid survival of Helicobacter pylori: How does urease activity trigger cytoplasmic pH homeostasis?
    • Stingl, K., Altendorf, K., and Bakker, E. P. (2002) Acid survival of Helicobacter pylori: how does urease activity trigger cytoplasmic pH homeostasis? Trends Microbiol. 10, 70-74.
    • (2002) Trends Microbiol , vol.10 , pp. 70-74
    • Stingl, K.1    Altendorf, K.2    Bakker, E.P.3
  • 4
    • 0036091552 scopus 로고    scopus 로고
    • Energetics of Helicobacter pylori and its implications for the mechanism of urease-dependent acid tolerance at pH 1
    • Stingl, K., Uhlemann, E.-M., Schmid, R., Altendorf, K., and Bakker, E. P. (2002) Energetics of Helicobacter pylori and its implications for the mechanism of urease-dependent acid tolerance at pH 1. J. Bacteriol. 184, 3053-3060.
    • (2002) J. Bacteriol , vol.184 , pp. 3053-3060
    • Stingl, K.1    Uhlemann, E.-M.2    Schmid, R.3    Altendorf, K.4    Bakker, E.P.5
  • 5
    • 33748752035 scopus 로고    scopus 로고
    • Acidresponsive gene regulation in the human pathogen Helicobacter pylori
    • Pflock, M., Kennard, S., Finsterer, N., and Beier, D. (2006) Acidresponsive gene regulation in the human pathogen Helicobacter pylori. J. Biotechnol. 126, 52-60.
    • (2006) J. Biotechnol , vol.126 , pp. 52-60
    • Pflock, M.1    Kennard, S.2    Finsterer, N.3    Beier, D.4
  • 6
    • 0002377269 scopus 로고    scopus 로고
    • Mobley, H. L. T, Mendz, G. L, and Hazell, S. L, Eds, pp, ASM Press, Washington D.C
    • Mobley, H. L. T. (2001) in Urease, in Helicobacter pylori: Physiology and genetics (Mobley, H. L. T., Mendz, G. L., and Hazell, S. L., Eds.), pp 179-191, ASM Press, Washington D.C.
    • (2001) Urease, in Helicobacter pylori: Physiology and genetics , pp. 179-191
    • Mobley, H.L.T.1
  • 7
    • 0038203196 scopus 로고    scopus 로고
    • Nickel uptake and utilization by microorganisms
    • Mulrooney, S. B., and Hausinger, R. P. (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
  • 8
    • 0037195612 scopus 로고    scopus 로고
    • Molecular hydrogen as an energy source for Helicobacter pylori
    • Olson, J. W., and Maier, R. J. (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
  • 9
    • 0032953199 scopus 로고    scopus 로고
    • Cyclic AMP receptor protein and TyrR are required for acid pH and anaerobic induction of hyaB and aniC in Salmonella typhimurium
    • Park, K. R., Giard, J.-C., Eom, J. H., Bearson, S., and Foster, J. W. (1999) Cyclic AMP receptor protein and TyrR are required for acid pH and anaerobic induction of hyaB and aniC in Salmonella typhimurium. J. Bacteriol. 181, 689-694.
    • (1999) J. Bacteriol , vol.181 , pp. 689-694
    • Park, K.R.1    Giard, J.-C.2    Eom, J.H.3    Bearson, S.4    Foster, J.W.5
  • 10
    • 35748974830 scopus 로고    scopus 로고
    • Occurance, classification, and biological function of hydrogenases: An overview
    • Vignais, P. M., and Billoud, B. (2007) Occurance, classification, and biological function of hydrogenases: an overview. Chem. Rev. 107, 4206-4272.
    • (2007) Chem. Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 11
    • 33645228520 scopus 로고    scopus 로고
    • Microbial nickel metalloregulation: NikRs for nickel ions
    • Dosanjh, N. S., and Michel, S. L. J. (2006) Microbial nickel metalloregulation: NikRs for nickel ions. Curr. Opin. Chem. Biol. 10, 1-8.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 1-8
    • Dosanjh, N.S.1    Michel, S.L.J.2
  • 12
    • 34248656478 scopus 로고    scopus 로고
    • Nickel-binding and accessory proteins facilitating Ni-enzyme maturation in Helicobacter pylori
    • Maier, R. J., Benoit, S., and Seshadri, S. (2007) Nickel-binding and accessory proteins facilitating Ni-enzyme maturation in Helicobacter pylori. BioMetals 20, 655-664.
    • (2007) BioMetals , vol.20 , pp. 655-664
    • Maier, R.J.1    Benoit, S.2    Seshadri, S.3
  • 13
    • 34248681553 scopus 로고    scopus 로고
    • Metal-responsive gene regulation and metal transport in Helicobacter species
    • Belzer, C., Stoof, J., and van Vliet, A. H. (2007) Metal-responsive gene regulation and metal transport in Helicobacter species. BioMetals 20, 417-429.
    • (2007) BioMetals , vol.20 , pp. 417-429
    • Belzer, C.1    Stoof, J.2    van Vliet, A.H.3
  • 15
    • 0042065267 scopus 로고    scopus 로고
    • Characterization of the roles of NikR, a nickelresponsive 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 nickelresponsive 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
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: Variations on a theme
    • Schreiter, E. R., and Drennan, C. L. (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
  • 17
    • 0842305636 scopus 로고    scopus 로고
    • Acid-responsive gene induction of ammoniaproducing enzymes in Helicobacter pylori is mediated via a metalresponsive repressor cascade
    • van Vliet, A. H., Kuipers, E. J., Stoof, J., Poppelaars, S. W., and Kusters, J. G. (2004) Acid-responsive gene induction of ammoniaproducing enzymes in Helicobacter pylori is mediated via a metalresponsive repressor cascade. Infect. Immun. 72, 766-773.
    • (2004) Infect. Immun , vol.72 , pp. 766-773
    • van Vliet, A.H.1    Kuipers, E.J.2    Stoof, J.3    Poppelaars, S.W.4    Kusters, J.G.5
  • 18
    • 3242881125 scopus 로고    scopus 로고
    • Responsiveness to acidity via metal ion regulators mediates virulence in the gastric pathogen Helicobacter pylori
    • Bury-Mone', S., Thiberge, J.-M., Contreras, M., Maitournam, A., Labigne, A., and De Reuse, H. (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
  • 19
    • 27744569940 scopus 로고    scopus 로고
    • The nickelresponsive 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 nickelresponsive 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
  • 20
    • 32444446916 scopus 로고    scopus 로고
    • Nickel represses the synthesis of the nickel permease NixA of Helicobacter pylori
    • Wolfram, L., Haas, E., and Bauerfeind, P. (2006) Nickel represses the synthesis of the nickel permease NixA of Helicobacter pylori. J. Bacteriol. 188, 1245-1250.
    • (2006) J. Bacteriol , vol.188 , pp. 1245-1250
    • Wolfram, L.1    Haas, E.2    Bauerfeind, P.3
  • 21
    • 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
  • 22
    • 33845505250 scopus 로고    scopus 로고
    • Helicobacter pylori HP1512 is a nickel-responsive NikR-regulated outer membrane protein
    • Davis, G. S., Flannery, E. L., and Mobley, H. L. T. (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.T.3
  • 23
    • 5644252852 scopus 로고    scopus 로고
    • NikRmediated regulation of Helicobacter pylori acid adaptation
    • van Vliet, A. H., Ernst, F. D., and Kusters, J. G. (2004) NikRmediated 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
  • 24
    • 0034970345 scopus 로고    scopus 로고
    • Regulation of transcription in Helicobacter pylori: Simple systems or complex circuits?
    • Scarlato, V., Delany, I., Spohn, G., and Beier, D. (2001) Regulation of transcription in Helicobacter pylori: simple systems or complex circuits? Int. J. Med. Microbiol. 291, 107-117.
    • (2001) Int. J. Med. Microbiol , vol.291 , pp. 107-117
    • Scarlato, V.1    Delany, I.2    Spohn, G.3    Beier, D.4
  • 25
    • 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
  • 26
    • 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
  • 27
    • 7444271910 scopus 로고    scopus 로고
    • A highperformance liquid chromatography method for determining transition metal content in proteins
    • Atanassova, A., Lam, R., and Zamble, D. B. (2004) A highperformance liquid chromatography method for determining transition metal content in proteins. Anal. Biochem. 335, 103-111.
    • (2004) Anal. Biochem , vol.335 , pp. 103-111
    • Atanassova, A.1    Lam, R.2    Zamble, D.B.3
  • 28
    • 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
  • 30
    • 3543072246 scopus 로고    scopus 로고
    • Metal-selective DNAbinding response of Escherichia coli NikR
    • Bloom, S. L., and Zamble, D. B. (2004) Metal-selective DNAbinding response of Escherichia coli NikR. Biochemistry 43, 10029-10038.
    • (2004) Biochemistry , vol.43 , pp. 10029-10038
    • Bloom, S.L.1    Zamble, D.B.2
  • 31
    • 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
  • 32
    • 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
  • 33
    • 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. 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
    • 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
  • 38
    • 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
  • 39
    • 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. (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
  • 41
    • 0034733505 scopus 로고    scopus 로고
    • Regulation of high affinity nickel uptake in bacteria
    • Chivers, P. T., and Sauer, R. T. (2000) Regulation of high affinity nickel uptake in bacteria. J. Biol. Chem. 275, 19735-19741.
    • (2000) J. Biol. Chem , vol.275 , pp. 19735-19741
    • Chivers, P.T.1    Sauer, R.T.2
  • 42
    • 47249162533 scopus 로고    scopus 로고
    • A histidinerich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from Helicobacter pylori: Implication for nickel homeostasis and bismuth susceptibility
    • Cun, S., Li, H., Ge, R., Lin, M. C., and Sun, H. (2008) A histidinerich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from Helicobacter pylori: implication for nickel homeostasis and bismuth susceptibility. J. Biol. Chem. 283, 15142-15151.
    • (2008) J. Biol. Chem , vol.283 , pp. 15142-15151
    • Cun, S.1    Li, H.2    Ge, R.3    Lin, M.C.4    Sun, H.5
  • 43
    • 51849097276 scopus 로고    scopus 로고
    • Binding of Ni(2+) to a histidine- and glutamine-rich protein, Hpn-like
    • Zeng, Y.-B., Zhang, D.-M., Li, H., and Sun, H. (2008) Binding of Ni(2+) to a histidine- and glutamine-rich protein, Hpn-like. J. Biol. Inorg. Chem. 13, 1121-1131.
    • (2008) J. Biol. Inorg. Chem , vol.13 , pp. 1121-1131
    • Zeng, Y.-B.1    Zhang, D.-M.2    Li, H.3    Sun, H.4
  • 44
    • 0029786121 scopus 로고    scopus 로고
    • pH-dependent enhancement of DNA binding by the ultrabithorax homeodomain
    • Li, L., von Kessler, D., Beachy, P. A., and Matthews, K. S. (1996) pH-dependent enhancement of DNA binding by the ultrabithorax homeodomain. Biochemistry 35, 9832-9839.
    • (1996) Biochemistry , vol.35 , pp. 9832-9839
    • Li, L.1    von Kessler, D.2    Beachy, P.A.3    Matthews, K.S.4
  • 45
    • 0025315476 scopus 로고
    • Proton-linked contributions to site-specific interactions of ? cI repressor and OR
    • Senear, D. F., and Ackers, G. K. (1990) Proton-linked contributions to site-specific interactions of ? cI repressor and OR. Biochemistry 29, 6568-6577.
    • (1990) Biochemistry , vol.29 , pp. 6568-6577
    • Senear, D.F.1    Ackers, G.K.2
  • 47
    • 0027522569 scopus 로고
    • Influence of pH on bacterial gene expression
    • Olson, E. R. (1993) Influence of pH on bacterial gene expression. Mol. Microbiol. 8, 5-14.
    • (1993) Mol. Microbiol , vol.8 , pp. 5-14
    • Olson, E.R.1
  • 48
    • 0028363850 scopus 로고
    • Control of the LexA regulon by pH: Evidence for a reversible inactivation of the LexA repressor during the growth cycle of Escherichia coli
    • Dri, A.-M., and Moreau, P. L. (1994) Control of the LexA regulon by pH: evidence for a reversible inactivation of the LexA repressor during the growth cycle of Escherichia coli. Mol. Microbiol. 12, 621-629.
    • (1994) Mol. Microbiol , vol.12 , pp. 621-629
    • Dri, A.-M.1    Moreau, P.L.2
  • 49
    • 0031054098 scopus 로고    scopus 로고
    • Preferential interactions of the Escherichia coli LexA repressor with anions and protons are coupled to binding the recA operator
    • Relan, N. K., Jenuwine, E. S., Gumbs, O. H., and Shaner, S. L. (1997) Preferential interactions of the Escherichia coli LexA repressor with anions and protons are coupled to binding the recA operator. Biochemistry 36, 1077-1084.
    • (1997) Biochemistry , vol.36 , pp. 1077-1084
    • Relan, N.K.1    Jenuwine, E.S.2    Gumbs, O.H.3    Shaner, S.L.4
  • 50
    • 0025741694 scopus 로고
    • Comparison of operator-specific and nonspecific DNA binding of the ? cI repressor: [KCl] and pH effects
    • Senear, D. F., and Batey, R. (1991) Comparison of operator-specific and nonspecific DNA binding of the ? cI repressor: [KCl] and pH effects. Biochemistry 30, 6677-6688.
    • (1991) Biochemistry , vol.30 , pp. 6677-6688
    • Senear, D.F.1    Batey, R.2
  • 53
    • 0028773287 scopus 로고
    • Electrostatic activation of Escherichia coli methionine repressor
    • Phillips, K., and Phillips, S. E. (1994) Electrostatic activation of Escherichia coli methionine repressor. Structure 2, 309-316.
    • (1994) Structure , vol.2 , pp. 309-316
    • Phillips, K.1    Phillips, S.E.2
  • 54
    • 0038781648 scopus 로고    scopus 로고
    • pH-regulated gene expression of the gastric pathogen Helicobacter pylori
    • Merrell, D. S., Goodrich, M. L., Otto, G., Tompkins, L. S., and Falkow, S. (2003) pH-regulated gene expression of the gastric pathogen Helicobacter pylori. Infect. Immun. 71, 3529-3539.
    • (2003) Infect. Immun , vol.71 , pp. 3529-3539
    • Merrell, D.S.1    Goodrich, M.L.2    Otto, G.3    Tompkins, L.S.4    Falkow, S.5
  • 55
    • 34249850789 scopus 로고    scopus 로고
    • Gene expression in vivo shows that Helicobacter pylori colonizes an acidic niche on the gastric surface
    • Scott, D. R., Marcus, E. A., Wen, Y., Oh, J., and Sachs, G. (2007) Gene expression in vivo shows that Helicobacter pylori colonizes an acidic niche on the gastric surface. Proc. Natl. Acad. Sci. U.S.A. 104, 7235-7240.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 7235-7240
    • Scott, D.R.1    Marcus, E.A.2    Wen, Y.3    Oh, J.4    Sachs, G.5
  • 56
    • 25444522923 scopus 로고    scopus 로고
    • Acid-induced activation of the urease promoters is mediated directly by the ArsRS two-component system of Helicobacter pylori
    • Pflock, M., Kennard, S., Delany, I., Scarlato, V., and Beier, D. (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.
    • (2005) Infect. Immun , vol.73 , pp. 6437-6445
    • Pflock, M.1    Kennard, S.2    Delany, I.3    Scarlato, V.4    Beier, D.5
  • 57
    • 0028177303 scopus 로고
    • DNA recognition by --sheets in the Arc repressor-operator crystal structure
    • Raumann, B. E., Rould, M. A., Pabo, C. O., and Sauer, R. T. (1994) DNA recognition by --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
  • 58
    • 0026641755 scopus 로고
    • Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands
    • Somers, W. S., and Phillips, S. E. (1992) Crystal structure of the met repressor-operator complex at 2.8 A resolution reveals DNA recognition by beta-strands. Nature 359, 387-393.
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, S.E.2
  • 59
    • 0028147466 scopus 로고
    • Major groove DNA recognition by --sheets: The ribbon-helix-helix family of gene regulatory proteins
    • Raumann, B. E., Brown, B. M., and Sauer, R. T. (1994) Major groove DNA recognition by --sheets: the ribbon-helix-helix family of gene regulatory proteins. Curr. Opin. Struct. Biol. 4, 36-43.
    • (1994) Curr. Opin. Struct. Biol , vol.4 , pp. 36-43
    • Raumann, B.E.1    Brown, B.M.2    Sauer, R.T.3
  • 60
    • 0024340022 scopus 로고
    • Identification of functionally important residues in the DNA binding region of the mnt repressor
    • Knight, K. L., and Sauer, R. T. (1989) Identification of functionally important residues in the DNA binding region of the mnt repressor. J. Biol. Chem. 264, 13706-13710.
    • (1989) J. Biol. Chem , vol.264 , pp. 13706-13710
    • Knight, K.L.1    Sauer, R.T.2
  • 61
    • 35148899681 scopus 로고    scopus 로고
    • Stress-induced mutagenesis in bacteria
    • Foster, P. L. (2007) Stress-induced mutagenesis in bacteria. Crit. Rev. Biochem. Mol. Biol. 42, 373-397.
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 373-397
    • Foster, P.L.1
  • 62
    • 0035724513 scopus 로고    scopus 로고
    • The Fur repressor controls transcription of iron-activated and -repressed genes in Helicobacter pylori
    • Delany, I., Spohn, G., Rappuoli, R., and Scarlato, V. (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
  • 63
    • 0344394987 scopus 로고    scopus 로고
    • An anti-repression Fur operator upstream of the promoter is required for iron-mediated transcriptional autoregulation in Helicobacter pylori
    • Delany, I., Spohn, G., Rappuoli, R., and Scarlato, V. (2003) An anti-repression Fur operator upstream of the promoter is required for iron-mediated transcriptional autoregulation in Helicobacter pylori. Mol. Microbiol. 50, 1329-1338.
    • (2003) Mol. Microbiol , vol.50 , pp. 1329-1338
    • Delany, I.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 64
    • 0032906661 scopus 로고    scopus 로고
    • The CtrA response regulator mediates temporal control of gene expression during the Caulobacter cell cycle
    • Reisenauer, A., Quon, K., and Shapiro, L. (1999) The CtrA response regulator mediates temporal control of gene expression during the Caulobacter cell cycle. J. Bacteriol. 181, 2430-2439.
    • (1999) J. Bacteriol , vol.181 , pp. 2430-2439
    • Reisenauer, A.1    Quon, K.2    Shapiro, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.