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The phenylpropanoidp -coumarate and structurally related aromatic compounds are produced in large amounts by green plants and are excellent carbon sources for many soil bacteria. Aerobic bacteria remove the acyl side chain from phenylpropanoids to leave an aromatic aldehyde, which then enters one of several possible central pathways of benzene ring degradation. We investigated the pathway for the anaerobic degradation ofp -coumarate by the phototrophic bacteriumRhodopseudomonas palustris and found that it also follows this metabolic logic. We characterized enzymes for the conversion ofp -coumarate top -hydroxybenzaldehyde and acetyl coenzyme A (acetyl-CoA) encoded by thecouAB operon. We also identified a MarR family transcriptional regulator that we named CouR. AcouR mutant had elevatedcouAB expression. In addition, His-tagged CouR bound with high affinity to a DNA fragment encompassing thecouAB promoter region, and binding was abrogated by the addition of nanomolar quantities ofp -coumaroyl-CoA but not byp -coumarate. Footprinting demonstrated binding of CouR to an inverted repeat sequence that overlaps the −10 region of thecouAB promoter. Our results provide evidence for binding of a CoA-modified aromatic compound by a MarR family member. Although the MarR family is widely distributed in bacteria and archaea and includes over 12,000 members, ligands have been identified for relatively few family members. Here we provide biochemical evidence for a new category of MarR ligand.

journal of bacteriology

Anaerobic <i>p</i> -Coumarate Degradation by Rhodopseudomonas palustris and Identification of CouR, a MarR Repressor Protein That Binds <i>p</i> -Coumaroyl Coenzyme A