Analysis of glycerol and dihydroxyacetone metabolism in Enterococcus faecium

Author:

Staerck Cindy1,Wasselin Valentin1,Budin-Verneuil Aurélie1,Rincé Isabelle1,Cacaci Margherita23,Weigel Markus4,Giraud Caroline1ORCID,Hain Torsten45,Hartke Axel1ORCID,Riboulet-Bisson Eliette1ORCID

Affiliation:

1. Normandie Univ, UNICAEN U2RM-Stress and Virulence, Esplanade de la Paix, 14032 Caen, France

2. Dipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario A. Gemelli IRCCS, Largo A. Gemelli 8, 00168 Rome, Italy

3. Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie, Università Cattolica del Sacro Cuore, Largo A. Gemelli 8, 00168 Rome, Italy

4. Institute of Medical Microbiology, Justus-Liebig-University Giessen, Biomedical Research Facility Seltersberg (BFS), Schubertstrasse 81, D-35392 Giessen, Germany

5. German Center for Infection Research (DZIF), Partner Site Giessen-Marburg-Langen, Schubertstrasse 81, D-35392 Giessen, Germany

Abstract

ABSTRACT Glycerol (Gly) can be dissimilated by two pathways in bacteria. Either this sugar alcohol is first oxidized to dihydroxyacetone (DHA) and then phosphorylated or it is first phosphorylated to glycerol-3-phosphate (GlyP) followed by oxidation. Oxidation of GlyP can be achieved by NAD-dependent dehydrogenases or by a GlyP oxidase. In both cases, dihydroxyacetone phosphate is the product. Genomic analysis showed that Enterococcus faecium harbors numerous genes annotated to encode activities for the two pathways. However, our physiological analyses of growth on glycerol showed that dissimilation is limited to aerobic conditions and that despite the presence of genes encoding presumed GlyP dehydrogenases, the GlyP oxidase is essential in this process. Although E. faecium contains an operon encoding the phosphotransfer protein DhaM and DHA kinase, which are required for DHA phosphorylation, it is unable to grow on DHA. This operon is highly expressed in stationary phase but its physiological role remains unknown. Finally, data obtained from sequencing of a transposon mutant bank of E. faecium grown on BHI revealed that the GlyP dehydrogenases and a major intrinsic family protein have important but hitherto unknown physiological functions.

Publisher

Oxford University Press (OUP)

Subject

Genetics,Molecular Biology,Microbiology

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