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Rhodobacter sphaeroides  strain 2.4.1 is a widely studied bacterium that has recently been shown to cleave the abundant marine anti-stress molecule dimethylsulfoniopropionate (DMSP) into acrylate plus gaseous dimethyl sulfide. It does so by using a lyase encoded by  dddL,  the promoter-distal gene of a three-gene operon,  acuR-acuI-dddL . Transcription of the operon was enhanced when cells were pre-grown with the substrate DMSP, but this induction is indirect, and requires the conversion of DMSP to the product acrylate, the  bona fide  co-inducer. This regulation is mediated by the product of the promoter-proximal gene  acuR,  a transcriptional regulator in the TetR family. AcuR represses the operon in the absence of acrylate, but this is relieved by the presence of the co-inducer. Another unusual regulatory feature is that the  acuR-acuI-dddL  mRNA transcript is leaderless, such that  acuR  lacks a Shine-Dalgarno ribosomal binding site and 5′-UTR, and is translated at a lower level compared to the downstream genes. This regulatory unit may be quite widespread in bacteria, since several other taxonomically diverse lineages have adjacent  acuR- like and  acuI- like genes; these operons also have no 5′ leader sequences or ribosomal binding sites and their predicted  cis- acting regulatory sequences resemble those of  R. sphaeroides acuR-acuI-dddL.

Unusual Regulation of a Leaderless Operon Involved in the Catabolism of Dimethylsulfoniopropionate in Rhodobacter sphaeroides