Sulfonate-sulfur utilization involves a portion of the assimilatory sulfate reduction pathway in Escherichia coli.
Strains of Escherichia coli lacking serine transacetylase or a positive regulator (Cys B protein) of the assimilatory sulfate reduction (ASR) pathway were unable to assimilate sulfonate-S, while single mutants in O-acetyl-L-serine sulfhydrylase (either 'A' or 'B') were able to do so. Mutants unable to reduce sulfate to sulfite were nonetheless able to form and accumulate sulfide and then cysteine from sulfonates, while strains lacking sulfite reductase were not. Thus terminal portions of the ASR pathway are involved in reduction of sulfonate-S to that of cysteine. E. coli K-12 formed cysteine more slowly, and accumulated lesser amounts of it with sulfonate-sulfur than it did from either sulfate or sulfite. These observations are consistent with our earlier report that sulfate is the preferred sulfur source when present simultaneously with a sulfonate.
Uria-Nickelsen
M R
MR
Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269-2131.
Leadbetter
E R
ER
Godchaux
W
W
D000123:Acetyltransferases / Q000235:genetics; D003545:Cysteine / Q000378:metabolism*; D003547:Cysteine Synthase / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D010084:Oxidation-Reduction; D051050:Serine O-Acetyltransferase; D013431:Sulfates / Q000378:metabolism*; D013451:Sulfonic Acids / Q000378:metabolism*
D013431:Sulfates; D013451:Sulfonic Acids; D000123:Acetyltransferases; D051050:Serine O-Acetyltransferase; D003547:Cysteine Synthase; D003545:Cysteine