Abstract

The C–S lyase aecD (MetC) from skin corynebacteria plays an important role in body odour formation by releasing odoriferous sulfanylalkanols from cysteine conjugates in human axilla secretions. The expression of the aecD gene from Corynebacterium jeikeium K411, a strain originally isolated from the human axilla, was down-regulated in cells grown in minimal medium supplemented with methionine. A candidate transcription regulator binding in front of the aecD coding region was detected by DNA affinity chromatography and identified as McbR by peptide mass fingerprinting. A 16-bp McbR-binding site was localized in the mapped promoter region of the aecD gene. The binding of purified McbR protein to the 16-bp sequence motif was demonstrated by DNA band shift assays. Comparative DNA microarray hybridizations and bioinformatic motif searches revealed the gene composition of the McbR regulon from C. jeikeium, including 28 genes that are organized in 16 transcription units. The McbR protein from C. jeikeium K411 directly regulates genes involved in methionine uptake and biosynthesis, in cysteine biosynthesis and sulfate reduction, and in the biosynthesis of amino acids belonging to the aspartate family.

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