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Volumn 46, Issue 48, 2007, Pages 13677-13683

Shewanella oneidensis MR-1 H-NOX regulation of a histidine kinase by nitric oxide

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONS; MAMMALS; NITRIC OXIDE; SENSORS;

EID: 36849072336     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7019035     Document Type: Article
Times cited : (78)

References (39)
  • 1
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer, L. M., Anantharaman, V., and Aravind, L. (2003) Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins, BMC Genomics 4, 5.
    • (2003) BMC Genomics , vol.4 , pp. 5
    • Iyer, L.M.1    Anantharaman, V.2    Aravind, L.3
  • 2
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • Karow, D. S., Pan, D., Tran, R., Pellicena, P., Presley, A., Mathies, R. A., and Marletta, M. A. (2004) Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis, Biochemistry 43, 10203-10211.
    • (2004) Biochemistry , vol.43 , pp. 10203-10211
    • Karow, D.S.1    Pan, D.2    Tran, R.3    Pellicena, P.4    Presley, A.5    Mathies, R.A.6    Marletta, M.A.7
  • 3
    • 0032902722 scopus 로고    scopus 로고
    • Guanylate cyclase and the NO/cgmp signaling pathway
    • Denninger, J. W., and Marletta, M. A. (1999) Guanylate cyclase and the NO/cgmp signaling pathway, Biochim. Biophys. Acta 1411, 334-350.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 334-350
    • Denninger, J.W.1    Marletta, M.A.2
  • 4
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005) A molecular basis for NO selectivity in soluble guanylate cyclase, Nat. Chem. Biol. 1, 53-59.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 5
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • Boon, E. M., and Marletta, M. A. (2005) Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins, Curr. Opin. Chem. Biol. 9, 441-446.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 441-446
    • Boon, E.M.1    Marletta, M.A.2
  • 6
    • 9444240366 scopus 로고    scopus 로고
    • Femtomolar sensitivity of a NO sensor from Clostridium botulinum
    • Nioche, P., Berka, V., Vipond, J., Minton, N., Tsai, A. L., and Raman, C. S. (2004) Femtomolar sensitivity of a NO sensor from Clostridium botulinum, Science 306, 1550-1553.
    • (2004) Science , vol.306 , pp. 1550-1553
    • Nioche, P.1    Berka, V.2    Vipond, J.3    Minton, N.4    Tsai, A.L.5    Raman, C.S.6
  • 7
    • 4444333687 scopus 로고    scopus 로고
    • Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases
    • Pellicena, P., Karow, D. S., Boon, E. M., Marletta, M. A., and Kuriyan, J. (2004) Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases, Proc. Natl. Acad. Sci. U.S.A. 101, 12854-12859.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 12854-12859
    • Pellicena, P.1    Karow, D.S.2    Boon, E.M.3    Marletta, M.A.4    Kuriyan, J.5
  • 9
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher, T., Helmann, J. D., and Unden, G. (2006) Stimulus perception in bacterial signal-transducing histidine kinases, Microbiol. Mol. Biol. Rev. 70, 910-938.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 10
    • 0025830353 scopus 로고
    • Reconstitution of the bacterial chemotaxis signal transduction system from purified components
    • Ninfa, E. G., Stock, A., Mowbray, S., and Stock, J. (1991) Reconstitution of the bacterial chemotaxis signal transduction system from purified components, J. Biol. Chem. 266, 9764-9770.
    • (1991) J. Biol. Chem , vol.266 , pp. 9764-9770
    • Ninfa, E.G.1    Stock, A.2    Mowbray, S.3    Stock, J.4
  • 11
    • 0036195221 scopus 로고    scopus 로고
    • Mechanism of regulation of the bifunctional histidine kinase ntrb in escherichia coli
    • Weiss, V., Kramer, G., Dunnebier, T., and Flotho, A. (2002) Mechanism of regulation of the bifunctional histidine kinase ntrb in escherichia coli, J. Mol. Microbiol. Biotechnol. 4, 229-233.
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 229-233
    • Weiss, V.1    Kramer, G.2    Dunnebier, T.3    Flotho, A.4
  • 12
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe, T. W., and Stock, J. B. (1999) The histidine protein kinase superfamily, Adv. Microb. Physiol. 41, 139-227.
    • (1999) Adv. Microb. Physiol , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 13
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H., and Stock, A. M. (2001) Histidine kinases and response regulator proteins in two-component signaling systems, Trends Biochem. Sci. 26, 369-376.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 14
    • 0036035414 scopus 로고    scopus 로고
    • Physiological role of the glnk signal transduction protein of escherichia coli: Survival of nitrogen starvation
    • Blauwkamp, T. A., and Ninfa, A. J. (2002) Physiological role of the glnk signal transduction protein of escherichia coli: Survival of nitrogen starvation, Mol. Microbiol. 46, 203-214.
    • (2002) Mol. Microbiol , vol.46 , pp. 203-214
    • Blauwkamp, T.A.1    Ninfa, A.J.2
  • 16
    • 0033580642 scopus 로고    scopus 로고
    • Mechanism of cheA protein kinase activation in receptor signaling complexes
    • Levit, M. N., Liu, Y., and Stock, J. B. (1999) Mechanism of cheA protein kinase activation in receptor signaling complexes, Biochemistry 38, 6651-6658.
    • (1999) Biochemistry , vol.38 , pp. 6651-6658
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 17
    • 0033527742 scopus 로고    scopus 로고
    • Inhibition of the fixL sensor kinase by the fixT protein in Sinorhizobium meliloti
    • Garnerone, A. M., Cabanes, D., Foussard, M., Boistard, P., and Batut, J. (1999) Inhibition of the fixL sensor kinase by the fixT protein in Sinorhizobium meliloti, J. Biol. Chem. 274, 32500-32506.
    • (1999) J. Biol. Chem , vol.274 , pp. 32500-32506
    • Garnerone, A.M.1    Cabanes, D.2    Foussard, M.3    Boistard, P.4    Batut, J.5
  • 19
    • 0030810454 scopus 로고    scopus 로고
    • Physiology and enzymology involved in denitrification by Shewanella putrefaciens
    • Krause, B., and Nealson, K. H. (1997) Physiology and enzymology involved in denitrification by Shewanella putrefaciens, Appl. Environ. Microbiol. 63, 2613-2618.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 2613-2618
    • Krause, B.1    Nealson, K.H.2
  • 20
    • 0022368856 scopus 로고
    • Dissimilatory nitrate reduction to nitrate, nitrous oxide, and ammonium by Pseudomonas putrefaciens
    • Samuelsson, M. O. (1985) Dissimilatory nitrate reduction to nitrate, nitrous oxide, and ammonium by Pseudomonas putrefaciens, Appl. Environ. Microbiol. 50, 812-815.
    • (1985) Appl. Environ. Microbiol , vol.50 , pp. 812-815
    • Samuelsson, M.O.1
  • 21
    • 0031472326 scopus 로고    scopus 로고
    • Localization of the heme binding region in soluble guanylate cyclase
    • Zhao, Y., and Marletta, M. A. (1997) Localization of the heme binding region in soluble guanylate cyclase, Biochemistry 36, 15959-15964.
    • (1997) Biochemistry , vol.36 , pp. 15959-15964
    • Zhao, Y.1    Marletta, M.A.2
  • 22
    • 0024219883 scopus 로고
    • Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor
    • Myers, C., and Nealson, K. H. (1988) Bacterial manganese reduction and growth with manganese oxide as the sole electron acceptor, Science 240, 1319-1321.
    • (1988) Science , vol.240 , pp. 1319-1321
    • Myers, C.1    Nealson, K.H.2
  • 23
    • 13944268797 scopus 로고    scopus 로고
    • A novel method for accurate operon predictions in all sequenced prokuryotes
    • Price, M. N., Huang, K. H., Alm, E. J., and Arkin, A. P. (2005) A novel method for accurate operon predictions in all sequenced prokuryotes, Nucleic Acids Res. 33, 880-892.
    • (2005) Nucleic Acids Res , vol.33 , pp. 880-892
    • Price, M.N.1    Huang, K.H.2    Alm, E.J.3    Arkin, A.P.4
  • 24
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states
    • Stone, J. R., and Marletta, M. A. (1994) Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbon monoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 25
    • 0027164115 scopus 로고
    • Purification and characterization of vanR and the cytosolic domain of vanS: A two-component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147
    • Wright, G. D., Holman, T. R., and Walsh, C. T. (1993) Purification and characterization of vanR and the cytosolic domain of vanS: A two-component regulatory system required for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 32, 5057-5063.
    • (1993) Biochemistry , vol.32 , pp. 5057-5063
    • Wright, G.D.1    Holman, T.R.2    Walsh, C.T.3
  • 26
    • 0027504131 scopus 로고
    • The essential tension: Opposed reactions in bacterial two-component regulatory systems
    • Russo, F. D., and Silhavy, T. J. (1993) The essential tension: Opposed reactions in bacterial two-component regulatory systems, Trends Microbiol. 1, 306-310.
    • (1993) Trends Microbiol , vol.1 , pp. 306-310
    • Russo, F.D.1    Silhavy, T.J.2
  • 27
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M., Huang, S. H., and Marletta, M. A. (2005) A molecular basis for NO selectivity in soluble guanylate cyclase, Nat. Chem. Biol. 1, 53-59.
    • (2005) Nat. Chem. Biol , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 28
    • 0031576335 scopus 로고    scopus 로고
    • Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface
    • Nohaile, M., Kern, D., Wemmer, D., Stedman, K., and Kustu, S. (1997) Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface, J. Mol. Biol. 273, 299-316.
    • (1997) J. Mol. Biol , vol.273 , pp. 299-316
    • Nohaile, M.1    Kern, D.2    Wemmer, D.3    Stedman, K.4    Kustu, S.5
  • 29
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B. F., Lipson, D., Wemmer, D. E., and Kern, D. (2001) Two-state allosteric behavior in a single-domain signaling protein, Science 291, 2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 30
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, M. A., Ditta, G. S., and Helinski, D. R. (1991) A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti, Nature 350, 170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 31
    • 0028964123 scopus 로고
    • The oxygen sensor protein, fixL, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation, and signal transduction
    • Monson, E. K., Ditta, G. S., and Helinski, D. R. (1995) The oxygen sensor protein, fixL, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation, and signal transduction, J. Biol. Chem. 270, 5243-5250.
    • (1995) J. Biol. Chem , vol.270 , pp. 5243-5250
    • Monson, E.K.1    Ditta, G.S.2    Helinski, D.R.3
  • 32
    • 0037663697 scopus 로고    scopus 로고
    • A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure
    • Dunham, C. M., Dioum, E. M., Tuckerman, J. R., Gonzalez, G., Scott, W. G., and Gilles-Gonzalez, M. A. (2003) A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure. Biochemistry 42, 7701-7708.
    • (2003) Biochemistry , vol.42 , pp. 7701-7708
    • Dunham, C.M.1    Dioum, E.M.2    Tuckerman, J.R.3    Gonzalez, G.4    Scott, W.G.5    Gilles-Gonzalez, M.A.6
  • 33
    • 0037076515 scopus 로고    scopus 로고
    • Ligand and oxidation-state specific regulation of the heme-based oxygen sensor fixL from Sinorhizobium meliloti
    • Tuckerman, J. R., Gonzalez, G., Dioum, E. M., and Gilles-Gonzalez, M. A. (2002) Ligand and oxidation-state specific regulation of the heme-based oxygen sensor fixL from Sinorhizobium meliloti, Biochemistry 41, 6170-6177.
    • (2002) Biochemistry , vol.41 , pp. 6170-6177
    • Tuckerman, J.R.1    Gonzalez, G.2    Dioum, E.M.3    Gilles-Gonzalez, M.A.4
  • 35
    • 14644401764 scopus 로고    scopus 로고
    • The complete denitrification pathway of the symbiotic, nitrogen-fixing bacterium Bradyrhizobium japonicum
    • Bedmar, E. J., Robles, E. F., and Delgado, M. J. (2005) The complete denitrification pathway of the symbiotic, nitrogen-fixing bacterium Bradyrhizobium japonicum, Biochem. Soc. Trans. 33, 141-144.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 141-144
    • Bedmar, E.J.1    Robles, E.F.2    Delgado, M.J.3
  • 36
    • 0042858242 scopus 로고    scopus 로고
    • Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the no-sensing regulator FNR, and flavohemoglobin HMP
    • Corker, H., and Poole, R. K. (2003) Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the no-sensing regulator FNR, and flavohemoglobin HMP, J. Biol. Chem. 278, 31584-31592.
    • (2003) J. Biol. Chem , vol.278 , pp. 31584-31592
    • Corker, H.1    Poole, R.K.2
  • 37
    • 85044710067 scopus 로고    scopus 로고
    • Dissimilatory metabolism of nitrogen oxides in bacteria: Comparative reconstruction of transcriptional networks
    • Rodionov, D. A., Dubchak, I. L., Arkin, A. P., Aim, E. J., and Gelfand, M. S. (2005) Dissimilatory metabolism of nitrogen oxides in bacteria: Comparative reconstruction of transcriptional networks, PLoS Comput. Biol. 1, e55.
    • (2005) PLoS Comput. Biol , vol.1
    • Rodionov, D.A.1    Dubchak, I.L.2    Arkin, A.P.3    Aim, E.J.4    Gelfand, M.S.5
  • 38
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks, B. C., Ferguson, S. J., Moir, J. W. B., and Richardson, D. J. (1995) Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions, Biochim. Biophys. Acta - Bioenergetics 1232, 97-173.
    • (1995) Biochim. Biophys. Acta - Bioenergetics , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 39
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. (1997) Cell biology and molecular basis of denitrification, Microbiol. Mol. Biol. Rev. 61, 533-616.
    • (1997) Microbiol. Mol. Biol. Rev , vol.61 , pp. 533-616
    • Zumft, W.G.1


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