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Microbiology. 2015 Nov;161(Pt 11):2232-42. doi: 10.1099/mic.0.000163. Epub 2015 Aug 25.

The metabolism of (R)-3-hydroxybutyrate is regulated by the enhancer-binding protein PA2005 and the alternative sigma factor RpoN in Pseudomonas aeruginosa PAO1.

Author information

1
1​Department of Chemistry, State University of New York - College of Environmental Science and Forestry, 1 Forestry Drive, Syracuse, New York, 13210, USA.
2
1​Department of Chemistry, State University of New York - College of Environmental Science and Forestry, 1 Forestry Drive, Syracuse, New York, 13210, USA 2​Center for Applied Microbiology, State University of New York - College of Environmental Science and Forestry, 1 Forestry Drive, Syracuse, New York, 13210, USA.

Abstract

A variety of soil-dwelling bacteria produce polyhydroxybutyrate (PHB), which serves as a source of energy and carbon under nutrient deprivation. Bacteria belonging to the genus Pseudomonas do not generally produce PHB but are capable of using the PHB degradation product (R)-3-hydroxybutyrate [(R)-3-HB] as a growth substrate. Essential to this utilization is the NAD+-dependent dehydrogenase BdhA that converts (R)-3-HB into acetoacetate, a molecule that readily enters central metabolism. Apart from the numerous studies that had focused on the biochemical characterization of BdhA, there was nothing known about the assimilation of (R)-3-HB in Pseudomonas, including the genetic regulation of bdhA expression. This study aimed to define the regulatory factors that govern or dictate the expression of the bdhA gene and (R)-3-HB assimilation in Pseudomonas aeruginosa PAO1. Importantly, expression of the bdhA gene was found to be specifically induced by (R)-3-HB in a manner dependent on the alternative sigma factor RpoN and the enhancer-binding protein PA2005.This mode of regulation was essential for the utilization of (R)-3-HB as a sole source of energy and carbon. However, non-induced levels of bdhA expression were sufficient for P. aeruginosa PAO1 to grow on ( ± )-1,3-butanediol, which is catabolized through an (R)-3-HB intermediate. Because this is, we believe, the first report of an enhancer-binding protein that responds to (R)-3-HB, PA2005 was named HbcR for (R)-3-hydroxybutyrate catabolism regulator.

PMID:
26311173
PMCID:
PMC4806590
DOI:
10.1099/mic.0.000163
[Indexed for MEDLINE]
Free PMC Article

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