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Volumn 437, Issue 7059, 2005, Pages 769-772

A non-haem iron centre in the transcription factor NorR senses nitric oxide

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; ENZYMES; ESCHERICHIA COLI; IRON; RNA;

EID: 26944499456     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature03953     Document Type: Article
Times cited : (259)

References (30)
  • 1
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith, O. W. & Stuehr, D. J. Nitric oxide synthases: properties and catalytic mechanism. Annu. Rev. Physiol. 57, 707-736 (1995).
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 3
    • 0033695033 scopus 로고    scopus 로고
    • A novel NO-responding regulator controls the reduction of nitric oxide in Ralstonia eutropha
    • Pohlmann, A., Cramm, R., Schmelz, K. & Friedrich, B. A novel NO-responding regulator controls the reduction of nitric oxide in Ralstonia eutropha. Mol. Microbiol. 38, 626-638 (2000).
    • (2000) Mol. Microbiol. , vol.38 , pp. 626-638
    • Pohlmann, A.1    Cramm, R.2    Schmelz, K.3    Friedrich, B.4
  • 4
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies
    • Fang, F. C. Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies. Nature Rev. Microbiol. 2, 820-832 (2004).
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 820-832
    • Fang, F.C.1
  • 5
    • 0037168511 scopus 로고    scopus 로고
    • Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron
    • D'Autréaux, B., Touati, D., Bersch, B., Latour, J. M. & Michaud-Soret, I. Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proc. Natl Acad. Sci. USA 99, 16619-16624 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16619-16624
    • D'Autréaux, B.1    Touati, D.2    Bersch, B.3    Latour, J.M.4    Michaud-Soret, I.5
  • 6
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator
    • Ding, H. G. & Demple, B. Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator. Proc. Natl Acad. Sci. USA 97, 5146-5150 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5146-5150
    • Ding, H.G.1    Demple, B.2
  • 7
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • Hausladen, A., Privalle, C. T., Keng, T., DeAngelo, J. & Stamler, J. S. Nitrosative stress: activation of the transcription factor OxyR. Cell 86, 719-729 (1996).
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    DeAngelo, J.4    Stamler, J.S.5
  • 8
    • 0036646484 scopus 로고    scopus 로고
    • NO sensing by FNR: Regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp
    • Cruz-Ramos, H. et al. NO sensing by FNR: regulation of the Escherichia coli NO-detoxifying flavohaemoglobin, Hmp. EMBO J. 21, 3235-3244 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3235-3244
    • Cruz-Ramos, H.1
  • 9
    • 1642514907 scopus 로고    scopus 로고
    • Prominent roles of the NorR and fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species
    • Mukhopadhyay, P., Zheng, M., Bedzyk, L. A., LaRossa, R. A. & Storz, G. Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. Proc. Natl Acad. Sci. USA 101, 745-750 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 745-750
    • Mukhopadhyay, P.1    Zheng, M.2    Bedzyk, L.A.3    LaRossa, R.A.4    Storz, G.5
  • 11
    • 0037332383 scopus 로고    scopus 로고
    • 54-dependent transcriptional activators
    • 54-dependent transcriptional activators. J. Bacteriol. 185, 1757-1767 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 1757-1767
    • Studholme, D.J.1    Dixon, R.2
  • 12
    • 4544366542 scopus 로고    scopus 로고
    • DNA binding activity of the Escherichia coli nitric oxide sensor NorR suggests a conserved target sequence in diverse Proteobacteria
    • Tucker, N. P., D'Autreaux, B., Studholme, D. J., Spiro, S. & Dixon, R. DNA binding activity of the Escherichia coli nitric oxide sensor NorR suggests a conserved target sequence in diverse Proteobacteria. J. Bacteriol. 186, 6656-6660 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 6656-6660
    • Tucker, N.P.1    D'Autreaux, B.2    Studholme, D.J.3    Spiro, S.4    Dixon, R.5
  • 13
    • 0037067737 scopus 로고    scopus 로고
    • A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin
    • Gomes, C. M. et al. A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin. J. Biol. Chem. 277, 25273-25276 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25273-25276
    • Gomes, C.M.1
  • 14
    • 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., Mandhana, N. & Spiro, S. 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).
    • (2002) J. Bacteriol. , vol.184 , pp. 4640-4643
    • Hutchings, M.I.1    Mandhana, N.2    Spiro, S.3
  • 16
    • 0037386522 scopus 로고    scopus 로고
    • Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
    • Clay, M. D., Cosper, C. A., Jenney, F. E. Jr, Adams, M. W. & Johnson, M. K. Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase. Proc. Natl Acad. Sci. USA 100, 3796-3801 (2003).
    • (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
  • 17
    • 0000689187 scopus 로고    scopus 로고
    • Structure and magnetic properties of trigonal bipyramidal iron nitrosyl complexes
    • Ray, M. et al. Structure and magnetic properties of trigonal bipyramidal iron nitrosyl complexes. Inorg. Chem. 38, 3110-3115 (1999).
    • (1999) Inorg. Chem. , vol.38 , pp. 3110-3115
    • Ray, M.1
  • 18
    • 0029168628 scopus 로고
    • 2 activation by non-heme iron enzyme active-sites
    • 2 activation by non-heme iron enzyme active-sites. J. Am. Chem. Soc. 117, 715-732 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 715-732
    • Brown, C.A.1
  • 20
    • 4243616042 scopus 로고
    • Principles of structure, bonding, and reactivity for metal nitrosyl complexes
    • Enemark, J. H. & Feltham, R. D. Principles of structure, bonding, and reactivity for metal nitrosyl complexes. Coord Chem. Rev. 13, 339-406 (1974).
    • (1974) Coord Chem. Rev. , vol.13 , pp. 339-406
    • Enemark, J.H.1    Feltham, R.D.2
  • 21
    • 0033938884 scopus 로고    scopus 로고
    • Isomerization of a binary sigma-promoter DNA complex by transcription activators
    • Cannon, W. V., Gallegos, M. T. & Buck, M. Isomerization of a binary sigma-promoter DNA complex by transcription activators. Nature Struct. Biol. 7, 594-601 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 594-601
    • Cannon, W.V.1    Gallegos, M.T.2    Buck, M.3
  • 22
    • 0036039734 scopus 로고    scopus 로고
    • Mechanochemical ATPases and transcriptional activation
    • Zhang, X. et al. Mechanochemical ATPases and transcriptional activation. Mol. Microbiol. 45, 895-903 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 895-903
    • Zhang, X.1
  • 23
    • 0026581288 scopus 로고
    • The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent
    • Austin, S. & Dixon, R. The prokaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 11, 2219-2228 (1992).
    • (1992) EMBO J. , vol.11 , pp. 2219-2228
    • Austin, S.1    Dixon, R.2
  • 24
    • 3042752919 scopus 로고    scopus 로고
    • Induction of nitric oxide release from the human alveolar epithelial cell line A549: An in vitro correlate of innate immune response to Mycobacterium tuberculosis
    • Roy, S., Sharma, S., Sharma, M., Aggarwal, R. & Bose, M. Induction of nitric oxide release from the human alveolar epithelial cell line A549: an in vitro correlate of innate immune response to Mycobacterium tuberculosis. Immunology 112, 471-480 (2004).
    • (2004) Immunology , vol.112 , pp. 471-480
    • Roy, S.1    Sharma, S.2    Sharma, M.3    Aggarwal, R.4    Bose, M.5
  • 25
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • Aravind, L. & Ponting, C. P. The GAF domain: an evolutionary link between diverse phototransducing proteins. Trends Biochem. Sci. 22, 458-459 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 26
    • 2442431645 scopus 로고    scopus 로고
    • Spectroscopic description of the two nitrosyl-iron complexes responsible for fur inhibition by nitric oxide
    • D'Autreaux, B. et al. Spectroscopic description of the two nitrosyl-iron complexes responsible for Fur inhibition by nitric oxide. J. Am. Chem. Soc. 126, 6005-6016 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6005-6016
    • D'Autreaux, B.1
  • 27
    • 0033592910 scopus 로고    scopus 로고
    • A molecular basis for nitric oxide sensing by soluble guanylate cyclase
    • Zhao, Y., Brandish, P. E., Ballou, D. P. & Marietta, M. A. A molecular basis for nitric oxide sensing by soluble guanylate cyclase. Proc. Natl Acad. Sci. USA 96, 14753-14758 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14753-14758
    • Zhao, Y.1    Brandish, P.E.2    Ballou, D.P.3    Marietta, M.A.4
  • 28
    • 0036644430 scopus 로고    scopus 로고
    • Pr(NO)]
    • Pr(NO)]. Inorg. Chem. 41, 3444-3456 (2002).
    • (2002) Inorg. Chem. , vol.41 , pp. 3444-3456
    • Li, M.1
  • 30
    • 0034669188 scopus 로고    scopus 로고
    • Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein
    • Little, R., Reyes-Ramirez, F., Zhang, Y., van Heeswijk, W. C. & Dixon, R. Signal transduction to the Azotobacter vinelandii NIFL-NIFA regulatory system is influenced directly by interaction with 2-oxoglutarate and the PII regulatory protein. EMBO J. 19, 6041-6050 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6041-6050
    • Little, R.1    Reyes-Ramirez, F.2    Zhang, Y.3    Van Heeswijk, W.C.4    Dixon, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.