1887

Abstract

There are two major pathways for methionine biosynthesis in micro-organisms. Little is known about these pathways in . The authors assigned a function to the (formerly ) and (formerly ) genes of by complementing and mutants, analysing the phenotype of and mutants, and carrying out enzyme activity assays. These genes encode polypeptides belonging to the cystathionine γ-synthase family of proteins. Interestingly, the MetI protein has both cystathionine γ-synthase and -acetylhomoserine thiolyase activities, whereas the MetC protein is a cystathionine β-lyase. In , the transsulfuration and the thiolation pathways are functional . Due to its dual activity, the MetI protein participates in both pathways. The and genes form an operon, the expression of which is subject to sulfur-dependent regulation. When the sulfur source is sulfate or cysteine the transcription of this operon is high. Conversely, when the sulfur source is methionine its transcription is low. An S-box sequence, which is located upstream of the gene, is involved in the regulation of the operon. Northern blot experiments demonstrated the existence of two transcripts: a small transcript corresponding to the premature transcription termination at the terminator present in the S-box and a large one corresponding to transcription of the complete operon. When methionine levels were limiting, the amount of the full-length transcript increased. These results substantiate a model of regulation by transcription antitermination.

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2002-02-01
2021-03-09
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