Metabolism of dimethylsulphoniopropionate by Ruegeria pomeroyi DSS‐3. Issue 4 (19th July 2013)

• Record Type: Journal Article
• Authors: Reisch, Chris R.; Crabb, Warren M.; Gifford, Scott M.; Teng, Quincy; Stoudemayer, Melissa J.; Moran, Mary Ann; Whitman, William B.
• Is Part Of: Molecular microbiology. Volume 89:Issue 4(2013)
• Page Start: 774
• Page End: 791
• Publication Date: 2013-07-19
• Subjects: Molecular microbiology -- Periodicals; 572.829
• DOI: 10.1111/mmi.12314
• Languages: English
• ISSNs: 0950-382X

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p> <italic>Ruegeria pomeroyi</italic> DSS‐3 possesses two general pathways for metabolism of dimethylsulphoniopropionate (DMSP), an osmolyte of algae and abundant carbon source for marine bacteria. In the DMSP cleavage pathway, acrylate is transformed into acryloyl‐CoA by propionate‐CoA ligase (SPO2934) and other unidentified acyl‐CoA ligases. Acryloyl‐CoA is then reduced to propionyl‐CoA by AcuI or SPO1914. Acryloyl‐CoA is also rapidly hydrated to 3‐hydroxypropionyl‐CoA by acryloyl‐CoA hydratase (SPO0147). A SPO1914 mutant was unable to grow on acrylate as the sole carbon source, supporting its role in this pathway. Similarly, growth on methylmercaptopropionate, the first intermediate of the DMSP demethylation pathway, was severely inhibited by a mutation in the gene encoding crotonyl‐CoA carboxylase/reductase, demonstrating that acetate produced by this pathway was metabolized by the ethylmalonyl‐CoA pathway. Amino acids and nucleosides from cells grown on <sup>13</sup>C‐enriched DMSP possessed labelling patterns that were consistent with carbon from DMSP being metabolized by both the ethylmalonyl‐CoA and acrylate pathways as well as a role for pyruvate dehydrogenase. This latter conclusion was supported by the phenotype of a <italic>pdh</italic> mutant, which grew poorly on electron‐rich substrates. Additionally, label from [<sup>13</sup>C‐methyl] DMSP only appeared in carbons derived from methyl‐tetrahydrofolate, and there was no evidence for a serine cycle of C‐1 assimilation.</p> </abstract>