Detecting envelope stress by monitoring β-barrel assembly

Seung-Hyun Cho, Joanna Szewczyk, Christina Pesavento, Matylda Zietek, Manuel Banzhaf, Paula Roszczenko, Abir Asmar, Géraldine Laloux, Ann-Kristin Hov, Pauline Leverrier, Charles Van der Henst, Didier Vertommen, Athanasios Typas, Jean-François Collet

Research output: Contribution to journalArticlepeer-review

105 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1652-64
Number of pages13
Issue number7
Publication statusPublished - 18 Dec 2014

Bibliographical note

Open Access under an Elsevier user licence


  • Amino 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
  • Journal Article
  • Research Support, Non-U.S. Gov't


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