Detecting envelope stress by monitoring β-barrel assembly.

TitleDetecting envelope stress by monitoring β-barrel assembly.
Publication TypeJournal Article
Year of Publication2014
AuthorsCho, S-H., J. Szewczyk, C. Pesavento, M. Zietek, M. Banzhaf, P. Roszczenko, A. Asmar, G. Laloux, A-K. Hov, P. Leverrier, C. Van der Henst, D. Vertommen, A. Typas, and J-F. Collet
Date Published2014 Dec 18
KeywordsAmino Acid Sequence, Bacterial Outer Membrane Proteins, Cell Membrane, Cell Wall, Escherichia coli, Escherichia coli Proteins, Membrane Proteins, Molecular Sequence Data, Protein Structure, Tertiary, Sequence Alignment, Signal Transduction

The cell envelope protects bacteria from their surroundings. Defects in its integrity or assembly are sensed by signal transduction systems, allowing cells to rapidly adjust. The Rcs phosphorelay responds to outer membrane (OM)- and peptidoglycan-related stress in enterobacteria. We elucidated how the OM lipoprotein RcsF, the upstream Rcs component, senses envelope stress and activates the signaling cascade. RcsF interacts with BamA, the major component of the β-barrel assembly machinery. In growing cells, BamA continuously funnels RcsF through the β-barrel OmpA, displaying RcsF on the cell surface. This process spatially separates RcsF from the downstream Rcs component, which we show is the inner membrane protein IgaA. The Rcs system is activated when BamA fails to bind RcsF and funnel it to OmpA. Newly synthesized RcsF then remains periplasmic, interacting with IgaA to activate the cascade. Thus RcsF senses envelope damage by monitoring the activity of the Bam machinery.

Alternate JournalCell
PubMed ID25525882
Research group: