메뉴 건너뛰기




Volumn 189, Issue 7, 2007, Pages 2743-2749

Characterization of the signaling domain of the NO-responsive regulator NorR from Ralstonia eutropha H16 by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE; NITRIC OXIDE REDUCTASE; PROTEIN NORA; PROTEIN NORB; PROTEIN NORR; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34147133176     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01865-06     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 2442418622 scopus 로고    scopus 로고
    • Rapid site-directed mutagenesis using two-PCR-generated DNA fragments reproducing the plasmid template
    • Allemandou, F., J. Nussberger, H. R. Brunner, and N. Brakch. 2003. Rapid site-directed mutagenesis using two-PCR-generated DNA fragments reproducing the plasmid template. J. Biomed. Biotechnol. 2003:202-207.
    • (2003) J. Biomed. Biotechnol , vol.2003 , pp. 202-207
    • Allemandou, F.1    Nussberger, J.2    Brunner, H.R.3    Brakch, N.4
  • 2
    • 31344459536 scopus 로고    scopus 로고
    • The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator
    • Bodenmiller, D. M., and S. Spiro. 2006. The yjeB (nsrR) gene of Escherichia coli encodes a nitric oxide-sensitive transcriptional regulator. J. Bacteriol. 188:874-881.
    • (2006) J. Bacteriol , vol.188 , pp. 874-881
    • Bodenmiller, D.M.1    Spiro, S.2
  • 3
    • 9244233838 scopus 로고    scopus 로고
    • A DNA region recognized by the nitric oxide-responsive transcriptional activator NorR is conserved in β- and γ-proteobacteria
    • Busch, A., A. Pohlmann, B. Friedrich, and R. Cramm. 2004. A DNA region recognized by the nitric oxide-responsive transcriptional activator NorR is conserved in β- and γ-proteobacteria. J. Bacteriol. 186:7980-7987.
    • (2004) J. Bacteriol , vol.186 , pp. 7980-7987
    • Busch, A.1    Pohlmann, A.2    Friedrich, B.3    Cramm, R.4
  • 5
    • 0037386522 scopus 로고    scopus 로고
    • Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
    • Clay, M. D., C. A. Cosper, F. E. Jenney, Jr., M. W. Adams, and M. K. Johnson. 2003. Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase. Proc. Natl. Acad. Sci. USA 100:3796-3801.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3796-3801
    • Clay, M.D.1    Cosper, C.A.2    Jenney Jr., F.E.3    Adams, M.W.4    Johnson, M.K.5
  • 6
    • 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 R. K. Poole. 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
  • 7
    • 0033528744 scopus 로고    scopus 로고
    • Reactions of nitric oxide with the reduced non-heme diiron center of the soluble methane monooxygenase hydroxylase
    • Coufal, D. E., P. Tavares, A. S. Pereira, B. H. Hyunh, and S. J. Lippard. 1999. Reactions of nitric oxide with the reduced non-heme diiron center of the soluble methane monooxygenase hydroxylase. Biochemistry 38:4504-4513.
    • (1999) Biochemistry , vol.38 , pp. 4504-4513
    • Coufal, D.E.1    Tavares, P.2    Pereira, A.S.3    Hyunh, B.H.4    Lippard, S.J.5
  • 8
    • 32544438794 scopus 로고    scopus 로고
    • NO-dependent transcriptional activation of gene expression in Ralstonia eutropha H16
    • Cramm, R., A. Büsch, and K. Strube. 2006. NO-dependent transcriptional activation of gene expression in Ralstonia eutropha H16. Biochem. Soc. Trans. 34:182-184.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 182-184
    • Cramm, R.1    Büsch, A.2    Strube, K.3
  • 9
    • 0030714062 scopus 로고    scopus 로고
    • Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16
    • Gramm, R., R. A. Siddiqui, and B. Friedrich. 1997. Two isofunctional nitric oxide reductases in Alcaligenes eutrophus H16. J. Bacteriol. 179:6769-6777.
    • (1997) J. Bacteriol , vol.179 , pp. 6769-6777
    • Gramm, R.1    Siddiqui, R.A.2    Friedrich, B.3
  • 10
    • 26944499456 scopus 로고    scopus 로고
    • A non-haem iron centre in the transcription factor NorR senses nitric oxide
    • D'Autreaux, B., N. P. Tucker, R. Dixon, and S. Spiro. 2005. A non-haem iron centre in the transcription factor NorR senses nitric oxide. Nature 437:769-772.
    • (2005) Nature , vol.437 , pp. 769-772
    • D'Autreaux, B.1    Tucker, N.P.2    Dixon, R.3    Spiro, S.4
  • 11
    • 0023645585 scopus 로고
    • Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 Å resolution
    • Frey, M., L. Sieker, F. Payan, R. Haser, M. Bruschi, G. Pepe, and J. LeGall. 1987. Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 Å resolution. J. Mol. Biol. 197:525-541.
    • (1987) J. Mol. Biol , vol.197 , pp. 525-541
    • Frey, M.1    Sieker, L.2    Payan, F.3    Haser, R.4    Bruschi, M.5    Pepe, G.6    LeGall, J.7
  • 13
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm, R. H., P. Kennepohl, and E. I. Solomon. 1996. Structural and functional aspects of metal sites in biology. Chem. Rev. 96:2239-2314.
    • (1996) Chem. Rev , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 14
    • 0025727991 scopus 로고
    • Expression of regulatory nif genes in Rhodobacter capsulatus
    • Hubner, P., J. C. Willison, P. M. Vignais, and T. A. Bickle. 1991. Expression of regulatory nif genes in Rhodobacter capsulatus. J. Bacteriol. 173:2993-2999.
    • (1991) J. Bacteriol , vol.173 , pp. 2993-2999
    • Hubner, P.1    Willison, J.C.2    Vignais, P.M.3    Bickle, T.A.4
  • 15
    • 0036330949 scopus 로고    scopus 로고
    • The NorR protein of Escherichia coli activates expression of the flavorubredoxin gene norV in response to reactive nitrogen species
    • Hutchings, M. I, N. Mandhana, and S. Spiro. 2002. The NorR protein of Escherichia coli activates expression of the flavorubredoxin gene norV in response to reactive nitrogen species. J. Bacteriol. 184:4640-4643.
    • (2002) J. Bacteriol , vol.184 , pp. 4640-4643
    • Hutchings, M.I.1    Mandhana, N.2    Spiro, S.3
  • 16
    • 0031461676 scopus 로고    scopus 로고
    • The extended environment of mononuclear metal centers in protein structures
    • Karlin, S., Z. Y. Zhu, and K. D. Karlin. 1997. The extended environment of mononuclear metal centers in protein structures. Proc. Natl. Acad. Sci. USA 94:14225-14230.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14225-14230
    • Karlin, S.1    Zhu, Z.Y.2    Karlin, K.D.3
  • 17
    • 0028228427 scopus 로고
    • The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation
    • Lenz, O., E. Schwartz, J. Dernedde, M. Eitinger, and B. Friedrich. 1994. The Alcaligenes eutrophus H16 hoxX gene participates in hydrogenase regulation. J. Bacteriol. 176:4385-4393.
    • (1994) J. Bacteriol , vol.176 , pp. 4385-4393
    • Lenz, O.1    Schwartz, E.2    Dernedde, J.3    Eitinger, M.4    Friedrich, B.5
  • 18
    • 71849104860 scopus 로고    scopus 로고
    • 17a.Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
    • 17a.Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
  • 20
    • 0034858690 scopus 로고    scopus 로고
    • Development of improved versatile broad-host-range vectors for use in methylotrophs and other Gram-negative bacteria
    • Marx, C. J., and M. E. Lidström. 2001. Development of improved versatile broad-host-range vectors for use in methylotrophs and other Gram-negative bacteria. Microbiology 147:2065-2075.
    • (2001) Microbiology , vol.147 , pp. 2065-2075
    • Marx, C.J.1    Lidström, M.E.2
  • 22
    • 0033695033 scopus 로고    scopus 로고
    • A novel NO-responding regulator controls the reduction of nitric oxide in Ralstonia eutropha
    • Pohlmann, A., R. Gramm, K. Schmelz, and B. Friedrich. 2000. A novel NO-responding regulator controls the reduction of nitric oxide in Ralstonia eutropha. Mol. Microbiol. 38:626-638.
    • (2000) Mol. Microbiol , vol.38 , pp. 626-638
    • Pohlmann, A.1    Gramm, R.2    Schmelz, K.3    Friedrich, B.4
  • 23
    • 85044710067 scopus 로고    scopus 로고
    • Rodionov, D. A., I. L. Dubchak, A. P. Arkin, E. J. Alm, and M. S. Gelfand. 2005. Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks. PLoS Comput. Biol. 1:e55.
    • Rodionov, D. A., I. L. Dubchak, A. P. Arkin, E. J. Alm, and M. S. Gelfand. 2005. Dissimilatory metabolism of nitrogen oxides in bacteria: comparative reconstruction of transcriptional networks. PLoS Comput. Biol. 1:e55.
  • 24
    • 34250969714 scopus 로고
    • A submersion method for culture of hydrogen-oxidizing bacteria: Growth physiological studies
    • Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. A submersion method for culture of hydrogen-oxidizing bacteria: growth physiological studies. Arch. Mikrobiol. 38:209-222.
    • (1961) Arch. Mikrobiol , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 25
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., U. B. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.B.2    Pühler, A.3
  • 26
    • 0037332383 scopus 로고    scopus 로고
    • 54-dependent transcriptional activators
    • 54-dependent transcriptional activators. J. Bacteriol. 185:1757-1767.
    • (2003) J. Bacteriol , vol.185 , pp. 1757-1767
    • Studholme, D.J.1    Dixon, R.2
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 0037074043 scopus 로고    scopus 로고
    • Kinetics, mechanism, and spectroscopy of the reversible binding of nitric oxide to aquated iron(II). An undergraduate text book reaction revisited
    • Wanat, A., T. Schneppensieper, G. Stochel, R. van Eldik, E. Bill, and K. Wieghardt. 2002. Kinetics, mechanism, and spectroscopy of the reversible binding of nitric oxide to aquated iron(II). An undergraduate text book reaction revisited. Inorg. Chem. 41:4-10.
    • (2002) Inorg. Chem , vol.41 , pp. 4-10
    • Wanat, A.1    Schneppensieper, T.2    Stochel, G.3    van Eldik, R.4    Bill, E.5    Wieghardt, K.6
  • 30
    • 0141503644 scopus 로고
    • The formation of an oxygen-binding flavohemoprotein from Alcaligenes eutrophus is plasmid-determined
    • Weihs, V., K. Schmidt, B. Schneider, and B. Friedrich. 1989. The formation of an oxygen-binding flavohemoprotein from Alcaligenes eutrophus is plasmid-determined. Arch. Microbiol. 151:546-550.
    • (1989) Arch. Microbiol , vol.151 , pp. 546-550
    • Weihs, V.1    Schmidt, K.2    Schneider, B.3    Friedrich, B.4
  • 31
    • 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
  • 32
    • 0036200207 scopus 로고    scopus 로고
    • Nitric oxide signaling and NO dependent transcriptional control in bacterial denitrification by members of the FNR-CRP regulator family
    • Zumft, W. G. 2002. Nitric oxide signaling and NO dependent transcriptional control in bacterial denitrification by members of the FNR-CRP regulator family. J. Mol. Microbiol. Biotechnol. 4:277-286.
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 277-286
    • Zumft, W.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.