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Subcellular localization, interactions and dynamics of the phage‐shock protein‐like Lia response in B acillus subtilis
Author(s) -
DomínguezEscobar Julia,
Wolf Diana,
Fritz Georg,
Höfler Carolin,
WedlichSöldner Roland,
Mascher Thorsten
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12586
Subject(s) - biology , cytoplasm , cell envelope , bacillus subtilis , operon , microbiology and biotechnology , inner membrane , response regulator , heat shock , membrane protein , biochemistry , heat shock protein , membrane , escherichia coli , genetics , bacteria , gene , bacterial protein , mitochondrion
Summary The liaIH operon of B acillus subtilis is the main target of the envelope stress‐inducible two‐component system LiaRS . Here, we studied the localization, interaction and cellular dynamics of Lia proteins to gain insights into the physiological role of the Lia response. We demonstrate that LiaI serves as the membrane anchor for the phage‐shock protein A homologue LiaH . Under non‐inducing conditions, LiaI locates in highly motile membrane‐associated foci, while LiaH is dispersed throughout the cytoplasm. Under stress conditions, both proteins are strongly induced and colocalize in numerous distinct static spots at the cytoplasmic membrane. This behaviour is independent of MreB and does also not correlate with the stalling of the cell wall biosynthesis machinery upon antibiotic inhibition. It can be induced by antibiotics that interfere with the membrane‐anchored steps of cell wall biosynthesis, while compounds that inhibit the cytoplasmic or extracytoplasmic steps do not trigger this response. Taken together, our data are consistent with a model in which the Lia system scans the cytoplasmic membrane for envelope perturbations. Upon their detection, LiaS activates the cognate response regulator LiaR , which in turn strongly induces the liaIH operon. Simultaneously, LiaI recruits LiaH to the membrane, presumably to protect the envelope and counteract the antibiotic‐induced damage.