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We have cloned and sequenced the 3-hydroxybutyrate dehydrogenase-encoding gene (bdhA ) fromRhizobium (Sinorhizobium) meliloti . The gene has an open reading frame of 777 bp that encodes a polypeptide of 258 amino acid residues (molecular weight 27,177, pI 6.07). TheR. meliloti Bdh protein exhibits features common to members of the short-chain alcohol dehydrogenase superfamily.bdhA is the first gene transcribed in an operon that also includesxdhA , encoding xanthine oxidase/dehydrogenase. Transcriptional start site analysis by primer extension identified two transcription starts. S1, a minor start site, was located 46 to 47 nucleotides upstream of the predicted ATG start codon, while S2, the major start site, was mapped 148 nucleotides from the start codon. Analysis of the sequence immediately upstream of either S1 or S2 failed to reveal the presence of any known consensus promoter sequences. Although a ς54 consensus sequence was identified in the region between S1 and S2, a corresponding transcript was not detected, and arpoN mutant ofR. meliloti was able to utilize 3-hydroxybutyrate as a sole carbon source. TheR. meliloti bdhA gene is able to confer uponEscherichia coli the ability to utilize 3-hydroxybutyrate as a sole carbon source. AnR. meliloti bdhA mutant accumulates poly-3-hydroxybutyrate to the same extent as the wild type and shows no symbiotic defects. Studies with a strain carrying alacZ transcriptional fusion tobdhA demonstrated that gene expression is growth phase associated.

journal of bacteriology

Poly-3-Hydroxybutyrate Degradation in <i>Rhizobium (Sinorhizobium) meliloti</i> : Isolation and Characterization of a Gene Encoding 3-Hydroxybutyrate Dehydrogenase

Poly-3-Hydroxybutyrate Degradation in Rhizobium (Sinorhizobium) meliloti : Isolation and Characterization of a Gene Encoding 3-Hydroxybutyrate Dehydrogenase