@article{mbs:/content/journal/micro/10.1099/mic.0.044776-0, author = "Fritsch, Frederike and Mauder, Norman and Williams, Tatjana and Weiser, Julia and Oberle, Markus and Beier, Dagmar", title = "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", journal= "Microbiology", year = "2011", volume = "157", number = "2", pages = "373-386", doi = "https://doi.org/10.1099/mic.0.044776-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.044776-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "qRT-PCR, quantitative real-time PCR", keywords = "RR, response regulator", keywords = "IM-HK, intramembrane-sensing histidine kinase", keywords = "EMSA, electrophoretic mobility shift assay", keywords = "HK, histidine kinase", keywords = "TCS, two-component system", keywords = "5′-RACE, rapid amplification of 5′ cDNA ends", abstract = "Most members of the phylum Firmicutes harbour a two-component system (TCS), 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 has been shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR orthologue of Listeria monocytogenes (LiaSR Lm ). Whole-genome transcriptional profiling indicated that activation of LiaSR Lm results in a remodelling of the cell envelope via the massive upregulation of membrane-associated and extracytoplasmic proteins in the presence of inducing stimuli. As shown for other LiaSR TCSs, LiaSR Lm is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaR Lm , which is required for the induction of the LiaSR Lm regulon, is controlled by the interplay between the histidine kinase and phosphatase activities of the bifunctional sensor protein LiaS Lm . Our data suggest that the phosphatase activity of LiaS Lm is stimulated by LiaF Lm in the absence of cell envelope stress.", }