Genomes and Genes
Gene Symbol: cysJ
Description: sulfite reductase, alpha subunit, flavoprotein
Alias: ECK2759, JW2734
Species: Escherichia coli str. K-12 substr. MG1655
- 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. ..
- 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...
- Kemp J, Atkinson D, Ehret A, Lazzarini R. EVIDENCE FOR THE IDENTITY OF THE NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE-SPECIFIC SULFITE AND NITRITE REDUCTASES OF ESCHERICHIA COLI. J Biol Chem. 1963;238:3466-71 pubmed
- 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. ..
- 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. ..
- 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. ..
- 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
- 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
- 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...
- 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 pubmedDNA from each of two specialized transducing lambda phage, lambda dcysJIHD and lambda cysJ, has been analysed by heteroduplex mapping...
- 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.
- 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. ..
- 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 ..
- Lazzarini R, Atkinson D. A triphosphopyridine nucleotide-specific nitrite reductase from Escherichia coli. J Biol Chem. 1961;236:3330-5 pubmed
- Loudon J, Loughlin R. Mutagenesis and regulation of the cysJ promoter of Escherichia coli K-12. Gene. 1992;122:17-25 pubmedThe 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...
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- 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. ..
- Bairoch A, Boeckmann B. The SWISS-PROT protein sequence data bank, recent developments. Nucleic Acids Res. 1993;21:3093-6 pubmed
- 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 ..
- 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
- 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
- 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