1887

Abstract

A gene encoding a serine acetyltransferase (SAT) potentially involved in the biosynthesis of cysteine was identified ∼4 kb upstream of the previously described gene cluster that encodes an amino acid permease in strain 3841. The gene exhibits >40% identity to the family of SATs containing N-terminal extensions that have been described for other bacteria and plants. The ORF has three possible translation initiation sites which potentially encode polypeptides of 311, 277 and/or 259 amino acid residues, respectively. All three ORFs complemented the mutation in an cysteine auxotroph, strain JM39. Insertion of Tn into in the genome of (strain RU632) lowered SAT activity in crude extracts by >95%. However, RU632 was not a cysteine auxotroph, which suggests that possesses some redundancy in cysteine biosynthesis. Additional copies of could not be detected in the genome when the gene was used as a hybridization probe. Therefore it is possible that possesses an alternative pathway for cysteine biosynthesis which avoids -acetylserine. Strain RU632 was unaffected in its ability to nodulate , and the nodules were effective for N fixation (measured by CH reduction). Transcriptional activity of was determined by measuring the β-galactosidase arising from ::Tn fusions. Maximal levels of expression were observed during early exponential growth and were not influenced by the level of sulphur (supplied as sulphate). However, transcription was repressed by approximately twofold in ammonium-grown, as opposed to glutamate-grown, cultures. Repression by ammonium was not seen in a strain defective for .

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2001-09-01
2024-04-19
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