Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis

MPG-Autoren
/persons/resource/persons77901

Dominguez-Escobar,  Julia
Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78862

Wedlich-Söldner,  Roland
Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Dominguez-Escobar, J., Wolf, D., Fritz, G., Höfler, C., Wedlich-Söldner, R., & Mascher, T. (2014). Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis. MOLECULAR MICROBIOLOGY, 92(4), 716-732. doi:10.1111/mmi.12586.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-CDF9-C
Zusammenfassung
The liaIH operon of Bacillus 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.