Primary structure of the assimilatory-type sulfite reductase from Desulfovibrio vulgaris (Hildenborough): cloning and nucleotide sequence of the reductase gene

Abstract

The nucleotide sequence encoding the structural gene (651 bp) and flanking regions for the assimilatory-type sulfite reductase from the sulfate-reducing bacterium Desulfovibrio vulgaris (Hildenborough) was determined after cloning a 1.4 kb HindIII/SalI genomic fragment possessing the gene into Bluescript pBS(+)KS. The primary structure of the protein was deduced, and the molecular mass of the apoprotein was estimated as 24 kDa. The amino acid sequence of the polypeptide shows some similarities at putative [Fe4S4] cluster binding sites in comparison with the heme protein subunit of the larger Escherichia coli and Salmonella typhimurium sulfite reductases and spinach nitrite reductase. This is the first reported sequence of a member of a new class of low molecular weight assimilatory sulfite-reducing enzymes recently identified in a number of anaerobic bacteria [Moura, I., Lina, A. R., Moura, J. J. G., Xavier, A. V., Fauque, G., Peck, H. D., & Le Gall, J. (1986) Biochem. Biophys. Res. Commun. 141, 1032-1041].

The third subunit of desulfoviridin‐type dissimilatory sulfite reductases

“…Comparison of the sequences of the lowmolecular-mass assimilatory sulfite reductase from Desulfbvihrio vulgaris (Hildenborough) [19] and the oligomeric assimilatory sulfite reductases from Escherichiu coli and Sulmonellu typhimuriurn 1201 revealed no significant similarity. Further comparison of primary structures has to await sequencing of dissimilatory enzymes.…”

Expression of the γ‐subunit gene of desulfoviridin‐type dissimilatory sulfite reductase and of the α‐ and β‐subunit genes is not coordinately regulated

“…The finding that the dsvC gene, located on a 3.5-kb SacII fragment, is transcribed in both Escherichia coli and Desulfovihrio vulgaris as an mRNA of only 400-600 nucleotides, and that both the dsvA and dsvB genes are present on a 7. (66 kDa) subunits of the a&, assimilatory sulfite reductase from Salmonella typhimurium and Escherichia coli [l 1, 121, and the gene encoding the low-molecular-mass (24 kDa) assimilatory sulfite reductase of Desulfovibrio vulgaris Hildenborough [13]. Gene sequences and regulation of expression were also reported for asrA, asrB and asrC, encoding polypeptides of 4O,31 and 37 kDa, respectively, which form the sulfite reductase of S. typhiniurium [14], capable of reducing sulfite to sulfide under anaerobic conditions.…”

“…At present the complete amino acid sequences of these subunits are not known, although their NHz-terminal sequences have been published [2]. On the contrary, extensive sequence information is available for the [13]. Gene sequences and regulation of expression were also reported for asrA, asrB and asrC, encoding polypeptides of 4O,31 and 37 kDa, respectively, which form the sulfite reductase of S. typhiniurium [14], capable of reducing sulfite to sulfide under anaerobic conditions.…”

Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens

“…Indeed, nothing on enzymes involved in dissimilatory sulfur oxidation in any of the primary domains has been published. The only sequences available for sulfur-metabolizing enzymes are from the polysulfide reductase of Wolinella succinogenes (11), bovine liver rhodanese (21), and the phosphoadenylsulfate reductase pathways of assimilatory sulfate reduction of Eschenichia coli (7,12), Salmonella typhimunium (14,15), and Desulfovibnio vulgaris (27).…”