메뉴 건너뛰기




Volumn 109, Issue 39, 2012, Pages 15734-15739

Reversible cycling between cysteine persulfide-ligated [2Fe-2S] and cysteine-ligated [4Fe-4S] clusters in the FNR regulatory protein

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; OXYGEN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84866876886     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208787109     Document Type: Article
Times cited : (96)

References (44)
  • 1
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • DOI 10.1016/S0168-6445(05)80007-5
    • Spiro S, Guest JR (1990) FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol Rev 6:399-428. (Pubitemid 20281613)
    • (1990) FEMS Microbiology Reviews , vol.75 , Issue.4 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 3
    • 33646184857 scopus 로고    scopus 로고
    • A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth
    • DOI 10.1074/jbc.M512312200
    • Constantinidou C, et al. (2006) A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth. J Biol Chem 281:4802-4815. (Pubitemid 43847742)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 4802-4815
    • Constantinidou, C.1    Hobman, J.L.2    Griffiths, L.3    Patel, M.D.4    Penn, C.W.5    Cole, J.A.6    Overton, T.W.7
  • 4
    • 59149095309 scopus 로고    scopus 로고
    • Signal perception by FNR: The role of the iron-sulfur cluster
    • Crack JC, et al. (2008) Signal perception by FNR: The role of the iron-sulfur cluster. Biochem Soc Trans 36:1144-1148.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1144-1148
    • Crack, J.C.1
  • 6
    • 0038352097 scopus 로고    scopus 로고
    • The role of Fe-S proteins in sensing and regulation in bacteria
    • DOI 10.1016/S1369-5274(03)00039-0
    • Kiley PJ, Beinert H (2003) The role of Fe-S proteins in sensing and regulation in bacteria. Curr Opin Microbiol 6:181-185. (Pubitemid 36628663)
    • (2003) Current Opinion in Microbiology , vol.6 , Issue.2 , pp. 181-185
    • Kiley, P.J.1    Beinert, H.2
  • 7
    • 79953298366 scopus 로고    scopus 로고
    • Iron-containing transcription factors and their roles as sensors
    • Fleischhacker AS, Kiley PJ (2011) Iron-containing transcription factors and their roles as sensors. Curr Opin Chem Biol 15:335-341.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 335-341
    • Fleischhacker, A.S.1    Kiley, P.J.2
  • 8
    • 0021103983 scopus 로고
    • Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli
    • Shaw DJ, Rice DW, Guest JR (1983) Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J Mol Biol 166:241-247.
    • (1983) J Mol Biol , vol.166 , pp. 241-247
    • Shaw, D.J.1    Rice, D.W.2    Guest, J.R.3
  • 9
    • 0027474352 scopus 로고
    • Properties of FNR proteins substituted at each of the five cysteine residues
    • Green J, Sharrocks AD, Green B, Geisow M, Guest JR (1993) Properties of FNR proteins substituted at each of the five cysteine residues. Mol Microbiol 8:61-68. (Pubitemid 23114822)
    • (1993) Molecular Microbiology , vol.8 , Issue.1 , pp. 61-68
    • Green, J.1    Sharrocks, A.D.2    Green, B.3    Geisow, M.4    Guest, J.R.5
  • 11
    • 0032457906 scopus 로고    scopus 로고
    • Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster
    • DOI 10.1016/S0168-6445(98)00022-9, PII S0168644598000229
    • Kiley PJ, Beinert H (1998) Oxygen sensing by the global regulator, FNR: The role of the iron-sulfur cluster. FEMS Microbiol Rev 22:341-352. (Pubitemid 29074341)
    • (1998) FEMS Microbiology Reviews , vol.22 , Issue.5 , pp. 341-352
    • Kiley, P.J.1    Beinert, H.2
  • 12
    • 0032505869 scopus 로고    scopus 로고
    • Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli
    • Popescu CV, Bates DM, Beinert H, Münck E, Kiley PJ (1998) Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli . Proc Natl Acad Sci USA 95:13431-13435.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13431-13435
    • Popescu, C.V.1    Bates, D.M.2    Beinert, H.3    Münck, E.4    Kiley, P.J.5
  • 13
    • 0027451092 scopus 로고
    • The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state
    • Lazazzera BA, Bates DM, Kiley PJ (1993) The activity of the Escherichia coli transcription factor FNR is regulated by a change in oligomeric state. Genes Dev 7:1993-2005. (Pubitemid 23312951)
    • (1993) Genes and Development , vol.7 , Issue.10 , pp. 1993-2005
    • Lazazzera, B.A.1    Bates, D.M.2    Kiley, P.J.3
  • 14
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • DOI 10.1074/jbc.271.5.2762
    • Lazazzera BA, Beinert H, Khoroshilova N, Kennedy MC, Kiley PJ (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. (Pubitemid 26047894)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.5 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 15
    • 1642453843 scopus 로고    scopus 로고
    • 2+ cluster of FNR from Escherichia coli
    • 2+ cluster of FNR from Escherichia coli. Biochemistry 43:791-798.
    • (2004) Biochemistry , vol.43 , pp. 791-798
    • Sutton, V.R.1
  • 17
    • 1542364538 scopus 로고    scopus 로고
    • Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR)
    • Crack JC, Green J, Thomson AJ (2004) Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR). J Biol Chem 279:9278- 9286.
    • (2004) J Biol Chem , vol.279 , pp. 9278-9286
    • Crack, J.C.1    Green, J.2    Thomson, A.J.3
  • 18
    • 33745833349 scopus 로고    scopus 로고
    • Detection of Sulfide Release from the Oxygen-sensing [4Fe-4S] Cluster of FNR
    • DOI 10.1074/jbc.C600042200
    • Crack JC, Green J, Le Brun NE, Thomson AJ (2006) Detection of sul fide release from the oxygen-sensing [4Fe-4S] cluster of FNR. J Biol Chem 281:18909-18913. (Pubitemid 44035392)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 18909-18913
    • Crack, J.C.1    Green, J.2    Le, B.N.E.3    Thomson, A.J.4
  • 20
    • 63849262301 scopus 로고    scopus 로고
    • 2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion
    • 2 sensitivity of the transcription factor FNR is controlled by Ser24 modulating the kinetics of [4Fe-4S] to [2Fe-2S] conversion. Proc Natl Acad Sci USA 106:4659-4664.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4659-4664
    • Jervis, A.J.1
  • 23
    • 0000088314 scopus 로고
    • 2H substitution: Coupling of Fe-S stretching and S-C-C bending modes
    • 2H substitution: Coupling of Fe-S stretching and S-C-C bending modes. J Am Chem Soc 111:3496-3504.
    • (1989) J Am Chem Soc , vol.111 , pp. 3496-3504
    • Han, S.1    Czernuszewicz, R.S.2    Spiro, T.G.3
  • 24
    • 0001164578 scopus 로고
    • 2 protein resonance Raman revisited: Structural variations among adrenodoxin, ferredoxin, and red paramagnetic protein
    • 2 protein resonance Raman revisited: Structural variations among adrenodoxin, ferredoxin, and red paramagnetic protein. J Am Chem Soc 111:3505-3511.
    • (1989) J Am Chem Soc , vol.111 , pp. 3505-3511
    • Han, S.1    Czernuszewicz, R.S.2    Kimura, T.3    Adams, M.W.W.4    Spiro, T.G.5
  • 25
    • 0026724952 scopus 로고
    • Resonance Raman and magnetic circular dichroism studies of reduced [2Fe-2S] proteins
    • Fu W, Drozdzewski PM, Davies MD, Sligar SG, Johnson MK (1992) Resonance Raman and magnetic circular dichroism studies of reduced [2Fe-2S] proteins. J Biol Chem 267: 15502-15510.
    • (1992) J Biol Chem , vol.267 , pp. 15502-15510
    • Fu, W.1    Drozdzewski, P.M.2    Davies, M.D.3    Sligar, S.G.4    Johnson, M.K.5
  • 26
    • 38949101397 scopus 로고    scopus 로고
    • 2+cluster switch in the transcriptional regulator FNR
    • 2+cluster switch in the transcriptional regulator FNR. J Am Chem Soc 130:1749-1758.
    • (2008) J Am Chem Soc , vol.130 , pp. 1749-1758
    • Crack, J.C.1
  • 27
    • 0021093573 scopus 로고
    • Resonance Raman spectroscopic evidence for a common [3Fe-4S] structure among proteins containing three-iron clusters
    • Johnson MK, Czernuszewicz RS, Spiro TG, Fee JA, Sweeney WV (1983) Resonance Raman spectroscopic evidence for a common [3Fe-4S] structure among proteins containing three-iron clusters. J Am Chem Soc 103:6671-6678.
    • (1983) J Am Chem Soc , vol.103 , pp. 6671-6678
    • Johnson, M.K.1    Czernuszewicz, R.S.2    Spiro, T.G.3    Fee, J.A.4    Sweeney, W.V.5
  • 31
    • 0033554009 scopus 로고    scopus 로고
    • Assembly of 2Fe-2S and 4Fe-4S clusters in the anaerobic ribonucleotide reductase from Escherichia coli
    • Ollagnier S, et al. (1999) Assembly of 2Fe-2S and 4Fe-4S clusters in the anaerobic ribonucleotide reductase from Escherichia coli. J Am Chem Soc 121:6344-6350.
    • (1999) J Am Chem Soc , vol.121 , pp. 6344-6350
    • Ollagnier, S.1
  • 33
    • 0017738617 scopus 로고    scopus 로고
    • Determination of hydrogen sulfide with 5,5′-dithiobis-(2- nitrobenzoicacid),N-ethylmaleimide, and parachloromercuribenzoate
    • Nashef AS, Osugo DT, Feeney RE (2004) Determination of hydrogen sulfide with 5,5′-dithiobis-(2-nitrobenzoicacid),N-ethylmaleimide, and parachloromercuribenzoate. Anal Biochem 79:394-405.
    • (2004) Anal Biochem , vol.79 , pp. 394-405
    • Nashef, A.S.1    Osugo, D.T.2    Feeney, R.E.3
  • 34
    • 0023952439 scopus 로고
    • 2- of aconitase during cluster interconversion and removal
    • 2- of aconitase during cluster interconversion and removal. J Biol Chem 263:8194-8198.
    • (1988) J Biol Chem , vol.263 , pp. 8194-8198
    • Kennedy, M.C.1    Beinert, H.2
  • 35
    • 34250187112 scopus 로고    scopus 로고
    • In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe - S] cluster scaffolding protein
    • DOI 10.1021/bi6026665
    • Unciuleac M-C, et al. (2007) In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry 46: 6812-6821. (Pubitemid 46906411)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6812-6821
    • Unciuleac, M.-C.1    Chandramouli, K.2    Naik, S.3    Mayer, S.4    Boi, H.H.5    Johnson, M.K.6    Dean, D.R.7
  • 39
    • 66949146078 scopus 로고    scopus 로고
    • IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
    • Tan G, Lu J, Bitoun JP, Huang H, Ding H (2009) IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions. Biochem J 420:463-472.
    • (2009) Biochem J , vol.420 , pp. 463-472
    • Tan, G.1    Lu, J.2    Bitoun, J.P.3    Huang, H.4    Ding, H.5
  • 40
    • 80955125480 scopus 로고    scopus 로고
    • Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins
    • Mühlenhoff U, Richter N, Pines O, Pierik AJ, Lill R (2011) Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins. J Biol Chem 286:41205-41216.
    • (2011) J Biol Chem , vol.286 , pp. 41205-41216
    • Mühlenhoff, U.1    Richter, N.2    Pines, O.3    Pierik, A.J.4    Lill, R.5
  • 41
    • 2142654882 scopus 로고    scopus 로고
    • Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
    • DOI 10.1042/BJ20031702
    • Ding H, Clark RJ (2004) Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein. Biochem J 379:433-440. (Pubitemid 38570116)
    • (2004) Biochemical Journal , vol.379 , Issue.2 , pp. 433-440
    • Ding, H.1    Clark, R.J.2
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 43
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.