Pseudomonas aeruginosa Ethanol Oxidation by AdhA in Low-Oxygen Environments.

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  • Additional Information
    • Source:
      Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1098-5530 (Electronic) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Washington, DC : American Society for Microbiology
    • Subject Terms:
    • Abstract:
      Pseudomonas aeruginosa has a broad metabolic repertoire that facilitates its coexistence with different microbes. Many microbes secrete products that P. aeruginosa can then catabolize, including ethanol, a common fermentation product. Here, we show that under oxygen-limiting conditions P. aeruginosa utilizes AdhA, an NAD-linked alcohol dehydrogenase, as a previously undescribed means for ethanol catabolism. In a rich medium containing ethanol, AdhA, but not the previously described PQQ-linked alcohol dehydrogenase, ExaA, oxidizes ethanol and leads to the accumulation of acetate in culture supernatants. AdhA-dependent acetate accumulation and the accompanying decrease in pH promote P. aeruginosa survival in LB-grown stationary-phase cultures. The transcription of adhA is elevated by hypoxia and under anoxic conditions, and we show that it is regulated by the Anr transcription factor. We have shown that lasR mutants, which lack an important quorum sensing regulator, have higher levels of Anr-regulated transcripts under low-oxygen conditions than their wild-type counterparts. Here, we show that a lasR mutant, when grown with ethanol, has an even larger decrease in pH than the wild type (WT) that is dependent on both anr and adhA The large increase in AdhA activity is similar to that of a strain expressing a hyperactive Anr-D149A variant. Ethanol catabolism in P. aeruginosa by AdhA supports growth on ethanol as a sole carbon source and electron donor in oxygen-limited settings and in cells growing by denitrification under anoxic conditions. This is the first demonstration of a physiological role for AdhA in ethanol oxidation in P. aeruginosa IMPORTANCE Ethanol is a common product of microbial fermentation, and the Pseudomonas aeruginosa response to and utilization of ethanol are relevant to our understanding of its role in microbial communities. Here, we report that the putative alcohol dehydrogenase AdhA is responsible for ethanol catabolism and acetate accumulation under low-oxygen conditions and that it is regulated by Anr.
      (Copyright © 2019 American Society for Microbiology.)
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    • Grant Information:
      P20 GM113132 United States GM NIGMS NIH HHS; T32 AI007519 United States AI NIAID NIH HHS; P30 CA023108 United States CA NCI NIH HHS; P30 DK117469 United States DK NIDDK NIH HHS; R01 GM108492 United States GM NIGMS NIH HHS; R01 AI091702 United States AI NIAID NIH HHS
    • Contributed Indexing:
      Keywords: AdhA; ExaA; Pseudomonas aeruginosa; ethanol; lasR
    • Accession Number:
      0 (Bacterial Proteins)
      0 (LasR protein, Pseudomonas aeruginosa)
      0 (Trans-Activators)
      142931-47-3 (ANR protein, Pseudomonas aeruginosa)
      3K9958V90M (Ethanol)
      EC 1.1.1.1 (Alcohol Dehydrogenase)
      Q40Q9N063P (Acetic Acid)
      S88TT14065 (Oxygen)
    • Publication Date:
      Date Created: 20190919 Date Completed: 20200609 Latest Revision: 20240721
    • Publication Date:
      20240721
    • Accession Number:
      PMC6832066
    • Accession Number:
      10.1128/JB.00393-19
    • Accession Number:
      31527114