Genomics

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The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm


ABSTRACT: Most members of the phylum Firmicutes harbor a two-component system, LiaSR, which is involved in the response to cell envelope stress elicited most notably by inhibitors of the lipid II cycle. In all LiaSR systems studied in detail LiaSR-mediated signal transduction was shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR homolog of Listeria monocytogenes (LiaSRLm). Whole genome transcriptional profiling indicated that activation of LiaSRLm results in a remodeling of the cell envelope via the massive upregulation of membrane or cell-wall associated proteins in the presence of inducing stimuli. As shown for other LiaSR two-component systems LiaSRLm is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaRLm, which is required for the induction of the LiaSRLm regulon, is controlled by the interplay between histidine kinase and phosphatase activity of the bifunctional sensor protein LiaSLm. Our data suggest that the phosphatase activity of LiaSLm is stimulated by LiaF in the absence of cell envelope stress

ORGANISM(S): Listeria monocytogenes Listeria monocytogenes EGD-e

PROVIDER: GSE24107 | GEO | 2010/11/16

SECONDARY ACCESSION(S): PRJNA130197

REPOSITORIES: GEO

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