Gene Symbol: cysJ
Description: sulfite reductase, alpha subunit, flavoprotein
Alias: ECK2759, JW2734
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Eschenbrenner M, Coves J, Fontecave M. NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. FEBS Lett. 1995;374:82-4 pubmed
    ..One can conclude that each alpha-chain of SiR-FP is composed of two distinct domains, one binding FAD and the other FMN and that the FMN-binding domains cooperate for a head-to-head subunit interaction. ..
  2. Brock J, Paz R, Cottle P, Janssen G. Naturally occurring adenines within mRNA coding sequences affect ribosome binding and expression in Escherichia coli. J Bacteriol. 2007;189:501-10 pubmed
    ..coli. Here we describe site-directed mutagenesis of the E. coli aroL, pncB, and cysJ coding sequences that was used to assess the contribution of naturally occurring adenines to in vivo expression and ..
  3. Sermon J, Vanoirbeek K, De Spiegeleer P, Van Houdt R, Aertsen A, Michiels C. Unique stress response to the lactoperoxidase-thiocyanate enzyme system in Escherichia coli. Res Microbiol. 2005;156:225-32 pubmed
    ..Several of the induced genes or pathways may be involved in bacterial defense against the toxic effects of the lactoperoxidase-thiocyanate enzyme system. ..
  4. Wu J, Siegel L, Kredich N. High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor. J Bacteriol. 1991;173:325-33 pubmed
    The flavoprotein and hemoprotein components of Escherichia coli B NADPH-sulfite reductase are encoded by cysJ and cysI, respectively...
  5. Ostrowski J, Wu J, Rueger D, Miller B, Siegel L, Kredich N. Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrit. J Biol Chem. 1989;264:15726-37 pubmed
    ..were determined and, together with previously reported data, confirmed the organization of this region as promoter-cysJ-cysI-cysH with all three genes oriented in the same direction from the promoter...
  6. Ostrowski J, Kredich N. Molecular characterization of the cysJIH promoters of Salmonella typhimurium and Escherichia coli: regulation by cysB protein and N-acetyl-L-serine. J Bacteriol. 1989;171:130-40 pubmed
    ..typhimurium is located 171 nucleotides upstream of the cysJ start codon. Minor start sites were found 8 and 9 nucleotides downstream of the major site...
  7. Fieschi F, Niviere V, Frier C, Decout J, Fontecave M. The mechanism and substrate specificity of the NADPH:flavin oxidoreductase from Escherichia coli. J Biol Chem. 1995;270:30392-400 pubmed
    ..coli growing cells. As a consequence, it can enhance the antiproliferative effect of hydroxyurea, a cell-specific ribonucleotide reductase inactivator. ..
  8. Coves J, Niviere V, Eschenbrenner M, Fontecave M. NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase. J Biol Chem. 1993;268:18604-9 pubmed
    ..Pure sulfite reductase has the ability to catalyze the reduction of free riboflavin, FMN, or FAD by NADPH and thus, as Fre, to transfer electrons to the iron center of metR2, a key step during the activation reaction. ..
  9. Murphy M, Siegel L, Kamin H, Rosenthal D. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. II. Identification of a new class of heme prosthetic group: an iron-tetrahydroporphyrin (isobacteriochlorin type) with eight carboxylic acid groups. J Biol Chem. 1973;248:2801-14 pubmed

More Information


  1. Sibille N, Blackledge M, Brutscher B, Coves J, Bersch B. Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. Biochemistry. 2005;44:9086-95 pubmed
    ..These observations are placed in the physiological context so they can contribute to the understanding of the electron transfer mechanism in the SiR holoenzyme. ..
  2. Ostrowski J, Barber M, Rueger D, Miller B, Siegel L, Kredich N. Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cyto. J Biol Chem. 1989;264:15796-808 pubmed
    ..b>cysJ, which codes for SiR-FP, was cloned from S. typhimurium LT7 and Escherichia coli B, and both genes were sequenced...
  4. Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer J, et al. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. J Mol Biol. 2000;299:199-212 pubmed
    ..Thus, a movement of the FMN-binding domain relative to the rest of the enzyme may be a requirement for its optimal positioning relative to both the FNR-like module and the beta-subunit. ..
  5. Gruez A, Zeghouf M, Bertrand J, Eschenbrenner M, Coves J, Fontecave M, et al. The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis. Acta Crystallogr D Biol Crystallogr. 1998;54:135-6 pubmed
    ..A solvent content of 75% was determined by a calibrated tetrachloromethane/toluene gradient which corresponds to three monomers per asymmetric unit. A 3 A resolution native data set was collected at beamline W32 of LURE, Orsay, France. ..
  6. Coves J, Eschenbrenner M, Fontecave M. Sulfite reductase of Escherichia coli is a ferrisiderophore reductase. Biochem Biophys Res Commun. 1993;192:1403-8 pubmed
    ..Free flavins, riboflavin, FMN, FAD were absolutely required, suggesting that this activity resides in the flavin reductase activity of sulfite reductase. ..
  7. Siegel L, Davis P. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components. J Biol Chem. 1974;249:1587-98 pubmed
  8. Siegel L, Murphy M, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups. J Biol Chem. 1973;248:251-64 pubmed
  9. Li C, Peck H, Przybyla A. Cloning of the 3'-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12. Gene. 1987;53:227-34 pubmed
    ..8.1.2)(cysI and cysJ) of Escherichia coli K-12 have been cloned by complementation. pCYSI contains two PstI fragments (18.3 and 2...
  10. Hunt C, Colless V, Smith M, Molasky D, Malo M, Loughlin R. Lambda transducing phage and clones carrying genes of the cysJIHDC gene cluster of Escherichia coli K12. J Gen Microbiol. 1987;133:2707-17 pubmed
    DNA from each of two specialized transducing lambda phage, lambda dcysJIHD and lambda cysJ, has been analysed by heteroduplex mapping...
  11. Tei H, Murata K, Kimura A. Molecular cloning of the cys genes (cysC, cysD, cysH, cysI, cysJ, and cysG) responsible for cysteine biosynthesis in Escherichia coli K-12. Biotechnol Appl Biochem. 1990;12:212-6 pubmed
    ..The following results were obtained. First, the cysCDHIJ regulon could be separated into cysCD and cysHIJ regions. Second, the cysG gene was quite different from the cysI and cysJ genes.
  12. Christner J, Munck E, Janick P, Siegel L. Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups. J Biol Chem. 1981;256:2098-101 pubmed
    ..Thus, sulfite reductase provides the first example of an active site where a heme and an iron-sulfur cluster are closely linked as a functional unit, probably via a common bridging ligand. ..
  13. Eschenbrenner M, Coves J, Fontecave M. The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. J Biol Chem. 1995;270:20550-5 pubmed
    ..A plasmid containing cysJ gene, coding for the alpha subunit, overexpresses flavin reductase activity by 100-fold, showing that alpha is the ..
  14. Lazzarini R, Atkinson D. A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli. J Biol Chem. 1961;236:3330-5 pubmed
  15. Loudon J, Loughlin R. Mutagenesis and regulation of the cysJ promoter of Escherichia coli K-12. Gene. 1992;122:17-25 pubmed
    The cysJ promoter of Escherichia coli K-12, which is positively controlled by the CysB regulatory protein, was localized through the formation of a fusion of cysJ, the gene encoding NADPH-cytochrome c reductase with lacZ...
  16. Coves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M. Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. Biochemistry. 1997;36:5921-8 pubmed
    ..Moreover, the FMN prosthetic group in SiR-FP23 and native SiR-FP is compared to that of cytochrome P450 reductase and bacterial cytochrome P450, which also contain one FAD and one FMN per polypeptide chain. ..
  17. Zeghouf M, Fontecave M, Macherel D, Coves J. The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors. Biochemistry. 1998;37:6114-23 pubmed
    ..Despite the conservation of the bi-flavin-domain structure between these proteins over evolutionary time, each of them provides significantly different flavin reactivities. ..
  18. Champier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J. Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain. Biochemistry. 2002;41:3770-80 pubmed
    ..The overall fold of SiR-FP18 is very similar to that of bacterial flavodoxins and of the flavodoxin-like domain in CPR or P450-BM3. ..
  19. Miller E, Jarboe L, Turner P, Pharkya P, Yomano L, York S, et al. Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180. Appl Environ Microbiol. 2009;75:6132-41 pubmed publisher
  20. Coves J, Lebrun C, Gervasi G, Dalbon P, Fontecave M. Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride. Biochem J. 1999;342 ( Pt 2):465-72 pubmed
    ..Taken together, our results have shown that flavoprotein inactivation by IDP is not a reliable indicator for a flavin radical intermediate in catalysis. ..
  21. Evrard A, Zeghouf M, Fontecave M, Roby C, Coves J. 31P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase. Eur J Biochem. 1999;261:430-7 pubmed
    ..This underlies some subtle differences between the two proteins for which a very similar overall structure is likely considering their common genetic origin and common operating cycle. ..
  22. Siegel L, Rueger D, Barber M, Krueger R, Orme Johnson N, Orme Johnson W. Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes. J Biol Chem. 1982;257:6343-50 pubmed
    ..The potential of the Fe4S4 center is approximately 70 mV more negative in the CN- as opposed to the CO-ligated HP (-420 mV), a result which indicates the presence of heme-Fe4S4-ligand interaction in the HP complexes. ..
  23. Bairoch A, Boeckmann B. The SWISS-PROT protein sequence data bank, recent developments. Nucleic Acids Res. 1993;21:3093-6 pubmed
  24. Gaudu P, Fontecave M. The NADPH: sulfite reductase of Escherichia coli is a paraquat reductase. Eur J Biochem. 1994;226:459-63 pubmed
    ..Since pure flavoprotein alpha subunit, encoded by the cysJ gene, has similar catalytic activities, it is suggested that paraquat receives electrons directly from the alpha ..
  25. Murphy M, Siegel L, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme. J Biol Chem. 1974;249:1610-4 pubmed
  26. Faeder E, Davis P, Siegel L. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleo. J Biol Chem. 1974;249:1599-609 pubmed
  27. Siegel L, Davis P, Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. J Biol Chem. 1974;249:1572-86 pubmed