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Volumn 60, Issue 6, 2006, Pages 1432-1445

Bacillus subtilis Fnr senses oxygen via a [4Fe-4S] cluster coordinated by three cysteine residues without change in the oligomeric state

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; CYSTEINE; FNR PROTEIN; IRON; NITRATE REDUCTASE; NITRITE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33744500236     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05198.x     Document Type: Article
Times cited : (52)

References (48)
  • 1
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert H. 1983 Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins. Anal Biochem 131: 373 378.
    • (1983) Anal Biochem , vol.131 , pp. 373-378
    • Beinert, H.1
  • 2
    • 0025857741 scopus 로고
    • Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R-26, and bovine heart mitochondria
    • Britt R.D. Sauer K. Klein M.P. Knaff D.B. Kriauciunas A. Yu C.A., et al. 1991 Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R-26, and bovine heart mitochondria. Biochemistry 30: 1892 1901.
    • (1991) Biochemistry , vol.30 , pp. 1892-1901
    • Britt, R.D.1    Sauer, K.2    Klein, M.P.3    Knaff, D.B.4    Kriauciunas, A.5    Yu, C.A.6
  • 3
    • 0001635420 scopus 로고
    • Transcriptional activation by Escherichia coli Crp protein
    • In. Mcknight, S.L. Yamamoto, K.R. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Crothers D.M. Steitz T.A. 1992 Transcriptional activation by Escherichia coli Crp protein. In Transcriptional Regulation. Mcknight S.L. Yamamoto K.R. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 501 534.
    • (1992) Transcriptional Regulation. , pp. 501-534
    • Crothers, D.M.1    Steitz, T.A.2
  • 4
    • 0028844507 scopus 로고
    • Anaerobic transcription activation in Bacillus subtilis: Identification of distinct FNR-dependent and -independent regulatory mechanisms
    • Cruz-Ramos H. Boursier L. Moszer I. Kunst F. Danchin A. Glaser P. 1995 Anaerobic transcription activation in Bacillus subtilis: identification of distinct FNR-dependent and -independent regulatory mechanisms. EMBO J 14: 5984 5994.
    • (1995) EMBO J , vol.14 , pp. 5984-5994
    • Cruz-Ramos, H.1    Boursier, L.2    Moszer, I.3    Kunst, F.4    Danchin, A.5    Glaser, P.6
  • 5
    • 17144398027 scopus 로고    scopus 로고
    • The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif
    • Eiting M. Hageluken G. Schubert W.D. Heinz D.W. 2005 The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif. Mol Microbiol 56: 433 446.
    • (2005) Mol Microbiol , vol.56 , pp. 433-446
    • Eiting, M.1    Hageluken, G.2    Schubert, W.D.3    Heinz, D.W.4
  • 6
    • 0027449175 scopus 로고
    • Activation of FNR-dependent transcription by iron: An in vitro switch for FNR
    • Green J. Guest J.R. 1993a Activation of FNR-dependent transcription by iron: an in vitro switch for FNR. FEMS Microbiol Lett 113: 219 222.
    • (1993) FEMS Microbiol Lett , vol.113 , pp. 219-222
    • Green, J.1    Guest, J.R.2
  • 7
    • 0027260768 scopus 로고
    • A role for iron in transcriptional activation by FNR
    • Green J. Guest J.R. 1993b A role for iron in transcriptional activation by FNR. FEBS Lett 329: 55 58.
    • (1993) FEBS Lett , vol.329 , pp. 55-58
    • Green, J.1    Guest, J.R.2
  • 8
    • 0027474352 scopus 로고
    • Properties of FNR proteins substituted at each of the five cysteine residues
    • Green J. Sharrocks A.D. Green B. Geisow M. Guest J.R. 1993 Properties of FNR proteins substituted at each of the five cysteine residues. Mol Microbiol 8: 61 68.
    • (1993) Mol Microbiol , vol.8 , pp. 61-68
    • Green, J.1    Sharrocks, A.D.2    Green, B.3    Geisow, M.4    Guest, J.R.5
  • 9
    • 0034982114 scopus 로고    scopus 로고
    • Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP
    • Green J. Scott C. Guest J.R. 2001 Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv Microb Physiol 44: 1 34.
    • (2001) Adv Microb Physiol , vol.44 , pp. 1-34
    • Green, J.1    Scott, C.2    Guest, J.R.3
  • 11
    • 0001947282 scopus 로고    scopus 로고
    • The FNR modulon and FNR-regulated gene expression
    • In. Lin, E.C. Lynch, A. (eds). New York, NY: Chapmann & Hall
    • Guest J.R. Green J. Irvine S. Spiro S. 1996 The FNR modulon and FNR-regulated gene expression. In Regulation of Gene Expression in Escherichia coli. Lin E.C. Lynch A. (eds). New York, NY: Chapmann & Hall, pp. 317 342.
    • (1996) Regulation of Gene Expression in Escherichia Coli. , pp. 317-342
    • Guest, J.R.1    Green, J.2    Irvine, S.3    Spiro, S.4
  • 14
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding
    • Khoroshilova N. Beinert H. Kiley P.J. 1995 Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc Natl Acad Sci USA 92: 2499 2503.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2499-2503
    • Khoroshilova, N.1    Beinert, H.2    Kiley, P.J.3
  • 15
    • 0031000271 scopus 로고    scopus 로고
    • Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity
    • Khoroshilova N. Popescu C. Munck E. Beinert H. Kiley P.J. 1997 Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity. Proc Natl Acad Sci USA 94: 6087 6092.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6087-6092
    • Khoroshilova, N.1    Popescu, C.2    Munck, E.3    Beinert, H.4    Kiley, P.J.5
  • 16
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster
    • Kiley P.J. Beinert H. 1998 Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster. FEMS Microbiol Rev 22: 341 352.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 17
    • 0025959037 scopus 로고
    • Fnr mutants that activate gene expression in the presence of oxygen
    • Kiley P.J. Reznikoff W.S. 1991 Fnr mutants that activate gene expression in the presence of oxygen. J Bacteriol 173: 16 22.
    • (1991) J Bacteriol , vol.173 , pp. 16-22
    • Kiley, P.J.1    Reznikoff, W.S.2
  • 18
    • 0026722419 scopus 로고
    • Allosteric changes in the cAMP receptor protein of Escherichia coli: Hinge reorientation
    • Kim J. Adhya S. Garges S. 1992 Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation. Proc Natl Acad Sci USA 89: 9700 9704.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9700-9704
    • Kim, J.1    Adhya, S.2    Garges, S.3
  • 19
    • 21744460379 scopus 로고    scopus 로고
    • Tolerance of the Rieske-type [2Fe-2S] cluster in recombinant ferredoxin BphA3 from Pseudomonas sp. KKS102 to histidine ligand mutations
    • Kimura S. Kikuchi A. Senda T. Shiro Y. Fukuda M. 2005 Tolerance of the Rieske-type [2Fe-2S] cluster in recombinant ferredoxin BphA3 from Pseudomonas sp. KKS102 to histidine ligand mutations. Biochem J 388: 869 878.
    • (2005) Biochem J , vol.388 , pp. 869-878
    • Kimura, S.1    Kikuchi, A.2    Senda, T.3    Shiro, Y.4    Fukuda, M.5
  • 20
    • 0344153756 scopus 로고    scopus 로고
    • Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: Exploiting the metabolic spectrum by controlling alternative gene programs
    • Körner H. Sofia H.J. Zumft W.G. 2003 Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol Rev 27: 559 592.
    • (2003) FEMS Microbiol Rev , vol.27 , pp. 559-592
    • Körner, H.1    Sofia, H.J.2    Zumft, W.G.3
  • 21
    • 0023710995 scopus 로고
    • Regulation of in vitro expression of the Escherichia coli frd operon: Alanine and Fnr represent positive and negative control elements
    • Latour D.J. Weiner J.H. 1988 Regulation of in vitro expression of the Escherichia coli frd operon: alanine and Fnr represent positive and negative control elements. Nucleic Acids Res 16: 6339 6352.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6339-6352
    • Latour, D.J.1    Weiner, J.H.2
  • 22
    • 23844452716 scopus 로고    scopus 로고
    • Radical S-Adenosylmethionine Enzyme Coproporphyrinogen III Oxidase HemN: Functional features of the [4Fe-4S] cluster and the two bound S-Adenosyl-L methionines
    • Layer G. Grage K. Teschner T. Schünemann V. Breckau D. Masoumi A., et al. 2005 Radical S-Adenosylmethionine Enzyme Coproporphyrinogen III Oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-Adenosyl-L methionines. J Biol Chem 280: 29038 29046.
    • (2005) J Biol Chem , vol.280 , pp. 29038-29046
    • Layer, G.1    Grage, K.2    Teschner, T.3    Schünemann, V.4    Breckau, D.5    Masoumi, A.6
  • 23
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera B.A. Beinert H. Khoroshilova N. Kennedy M.C. Kiley P.J. 1996 DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J Biol Chem 271: 2762 2768.
    • (1996) J Biol Chem , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 24
    • 0001064679 scopus 로고
    • Studies on the chemical nature of Clostridial ferredoxin
    • Lovenberg W. Buchanan B.B. Rabinowitz J.C. 1963 Studies on the chemical nature of Clostridial ferredoxin. J Biol Chem 238: 3899 3913.
    • (1963) J Biol Chem , vol.238 , pp. 3899-3913
    • Lovenberg, W.1    Buchanan, B.B.2    Rabinowitz, J.C.3
  • 25
    • 0033972849 scopus 로고    scopus 로고
    • Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions
    • Marino M. Hoffmann T. Schmid R. Mobitz H. Jahn D. 2000 Changes in protein synthesis during the adaptation of Bacillus subtilis to anaerobic growth conditions. Microbiology 146: 97 105.
    • (2000) Microbiology , vol.146 , pp. 97-105
    • Marino, M.1    Hoffmann, T.2    Schmid, R.3    Mobitz, H.4    Jahn, D.5
  • 26
    • 0035165629 scopus 로고    scopus 로고
    • Modulation of anaerobic energy metabolism of Bacillus subtilis by arfM (ywiD)
    • Marino M. Ramos H.C. Hoffmann T. Glaser P. Jahn D. 2001 Modulation of anaerobic energy metabolism of Bacillus subtilis by arfM (ywiD). J Bacteriol 183: 6815 6821.
    • (2001) J Bacteriol , vol.183 , pp. 6815-6821
    • Marino, M.1    Ramos, H.C.2    Hoffmann, T.3    Glaser, P.4    Jahn, D.5
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • Miller J.H. 1972 Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.H.1
  • 28
    • 0035824571 scopus 로고    scopus 로고
    • Characterization of the dimerization domain in the FNR transcription factor
    • Moore L.J. Kiley P.J. 2001 Characterization of the dimerization domain in the FNR transcription factor. J Biol Chem 276: 45744 45750.
    • (2001) J Biol Chem , vol.276 , pp. 45744-45750
    • Moore, L.J.1    Kiley, P.J.2
  • 30
    • 0035104390 scopus 로고    scopus 로고
    • Involvement of ResE phosphatase activity in down-regulation of ResD-controlled genes in Bacillus subtilis during aerobic growth
    • Nakano M.M. Zhu Y. 2001 Involvement of ResE phosphatase activity in down-regulation of ResD-controlled genes in Bacillus subtilis during aerobic growth. J Bacteriol 183: 1938 1944.
    • (2001) J Bacteriol , vol.183 , pp. 1938-1944
    • Nakano, M.M.1    Zhu, Y.2
  • 31
    • 0031727390 scopus 로고    scopus 로고
    • Anaerobic growth of a 'strict aerobe' (Bacillus subtilis)
    • Nakano M.M. Zuber P. 1998 Anaerobic growth of a 'strict aerobe' (Bacillus subtilis). Annu Rev Microbiol 52: 165 190.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 165-190
    • Nakano, M.M.1    Zuber, P.2
  • 32
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth of Bacillus subtilis: Identification of fermentation end products and genes required for growth
    • Nakano M.M. Dailly Y.P. Zuber P. Clark D.P. 1997 Characterization of anaerobic fermentative growth of Bacillus subtilis: identification of fermentation end products and genes required for growth. J Bacteriol 179: 6749 6755.
    • (1997) J Bacteriol , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 33
    • 0031691173 scopus 로고    scopus 로고
    • Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE
    • Nakano M.M. Hoffmann T. Zhu Y. Jahn D. 1998 Nitrogen and oxygen regulation of Bacillus subtilis nasDEF encoding NADH-dependent nitrite reductase by TnrA and ResDE. J Bacteriol 180: 5344 5350.
    • (1998) J Bacteriol , vol.180 , pp. 5344-5350
    • Nakano, M.M.1    Hoffmann, T.2    Zhu, Y.3    Jahn, D.4
  • 34
    • 0034671172 scopus 로고    scopus 로고
    • Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 a resolution
    • Passner J.M. Schultz S.C. Steitz T.A. 2000 Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution. J Mol Biol 304: 847 859.
    • (2000) J Mol Biol , vol.304 , pp. 847-859
    • Passner, J.M.1    Schultz, S.C.2    Steitz, T.A.3
  • 37
    • 0031746383 scopus 로고    scopus 로고
    • PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro
    • Qi Y. Hulett F.M. 1998 PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro. Mol Microbiol 28: 1187 1197.
    • (1998) Mol Microbiol , vol.28 , pp. 1187-1197
    • Qi, Y.1    Hulett, F.M.2
  • 39
    • 0031054113 scopus 로고    scopus 로고
    • A Gly145Ser substitution in the transcriptional activator PrfA causes constitutive overexpression of virulence factors in Listeria monocytogenes
    • Ripio M.T. Dominguez-Bernal G. Lara M. Suarez M. Vazquez-Boland J.A. 1997 A Gly145Ser substitution in the transcriptional activator PrfA causes constitutive overexpression of virulence factors in Listeria monocytogenes. J Bacteriol 179: 1533 1540.
    • (1997) J Bacteriol , vol.179 , pp. 1533-1540
    • Ripio, M.T.1    Dominguez-Bernal, G.2    Lara, M.3    Suarez, M.4    Vazquez-Boland, J.A.5
  • 40
    • 3242885293 scopus 로고    scopus 로고
    • The PredictProtein Server
    • (web server issue).
    • Rost B. Yachdav G. Liu L. 2004 The PredictProtein Server. Nucleic Acids Res 32: W321 326 (web server issue).
    • (2004) Nucleic Acids Res , vol.32
    • Rost, B.1    Yachdav, G.2    Liu, L.3
  • 41
    • 0025892985 scopus 로고
    • Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon
    • Rygus T. Hillen W. 1991 Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon. Appl Microbiol Biotechnol 35: 594 599.
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 594-599
    • Rygus, T.1    Hillen, W.2
  • 43
    • 0025914242 scopus 로고
    • Crystal structure of a CAP-DNA complex: The DNA is bent by 90 degrees
    • Schultz S.C. Shields G.C. Steitz T.A. 1991 Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees. Science 253: 1001 1007.
    • (1991) Science , vol.253 , pp. 1001-1007
    • Schultz, S.C.1    Shields, G.C.2    Steitz, T.A.3
  • 44
    • 0033910009 scopus 로고    scopus 로고
    • Structure and dynamics of biomolecules studied by Mössbauer spectroscopy
    • Schünemann V. Winkler H. 2000 Structure and dynamics of biomolecules studied by Mössbauer spectroscopy. Rep Prog Phys 63: 263 353.
    • (2000) Rep Prog Phys , vol.63 , pp. 263-353
    • Schünemann, V.1    Winkler, H.2
  • 45
    • 0025078440 scopus 로고
    • In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of Escherichia coli
    • Sharrocks A.D. Green J. Guest J.R. 1990 In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of Escherichia coli. FEBS Lett 270: 119 122.
    • (1990) FEBS Lett , vol.270 , pp. 119-122
    • Sharrocks, A.D.1    Green, J.2    Guest, J.R.3
  • 47
    • 0024397088 scopus 로고
    • Role of cysteine residues and of metal ions in the regulatory functioning of FNR, the transcriptional regulator of anaerobic respiration in Escherichia coli
    • Trageser M. Unden G. 1989 Role of cysteine residues and of metal ions in the regulatory functioning of FNR, the transcriptional regulator of anaerobic respiration in Escherichia coli. Mol Microbiol 3: 593 599.
    • (1989) Mol Microbiol , vol.3 , pp. 593-599
    • Trageser, M.1    Unden, G.2
  • 48
    • 0033891425 scopus 로고    scopus 로고
    • Global gene expression profiles of Bacillus subtilis grown under anaerobic conditions
    • Ye R.W. Tao W. Bedzyk L. Young T. Chen M. Li L. 2000 Global gene expression profiles of Bacillus subtilis grown under anaerobic conditions. J Bacteriol 182: 4458 4465.
    • (2000) J Bacteriol , vol.182 , pp. 4458-4465
    • Ye, R.W.1    Tao, W.2    Bedzyk, L.3    Young, T.4    Chen, M.5    Li, L.6


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