Glycine betaine loses its osmoprotective activity in a bspA strain of Erwinia chrysanthemi.
Erwinia chrysanthemi insertion mutants were isolated that grew poorly specifically in the presence of glycine betaine (GB) or its analogues in high-salt media. Transposon insertions were found to affect the bspA gene, which forms an operon including the psd locus coding for phosphatidylserine decarboxylase. Initial GB uptake is not affected by the bspA mutation. However, in high-salt medium, its initial accumulation is followed by a reduced glucose uptake and a release of GB but not a loss of viability. BspA is homologous to the widespread MscS channel, YggB, but does not seem to constitute a mechanosensitive channel. We suggest that BspA is a protein sensing both intracellular GB and the extracellular salt content of the medium, the hypothesis being built on the observation that BspA is necessary to maintain the GB pool during osmoadaptation in high-salt media containing this osmoprotectant.
Touzé
T
T
Osmorégulation chez les bactéries, CNRS UMR 6026, Université de Rennes I, Campus de Beaulieu, Av. du Général Leclerc, 35042 Rennes, France.
Gouesbet
G
G
Boiangiu
C
C
Jebbar
M
M
Bonnassie
S
S
Blanco
C
C
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001622:Betaine / Q000494:pharmacology*; D004251:DNA Transposable Elements / Q000235:genetics; D016974:Dickeya chrysanthemi / Q000187:drug effects* / Q000235:genetics / Q000502:physiology*; D005798:Genes, Bacterial; D005947:Glucose / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009876:Operon / Q000235:genetics; D010802:Phylogeny; D014882:Water-Electrolyte Balance / Q000502:physiology*
D001426:Bacterial Proteins; C105995:BspA protein, bacteria; D004251:DNA Transposable Elements; D008565:Membrane Proteins; D001622:Betaine; D005947:Glucose