A lipoprotein/b-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane

Anna Konovalova, Angela M. Mitchell, Thomas J. Silhavy

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

Lipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with b-barrel proteins (OMPs) allowing it to adopt a transmembrane orientation with a lipidated N-terminal domain on the cell surface and a periplasmic C-terminal domain. Here we report that mutations that remove BamE or alter a residue in the RcsF trans-lumen domain specifically prevent assembly of the interlocked complexes without inactivating either RcsF or the OMP. Using these mutations we demonstrate that these RcsF/OMP complexes are required for sensing OM outer leaflet stress. Using mutations that alter the positively charged surface-exposed domain, we show that RcsF monitors lateral interactions between lipopolysaccharide (LPS) molecules. When these interactions are disrupted by cationic antimicrobial peptides, or by the loss of negatively charged phosphate groups on the LPS molecule, this information is transduced to the RcsF C-terminal signaling domain located in the periplasm to activate the stress response.

Original languageEnglish (US)
Article numbere15276
JournaleLife
Volume5
Issue numberJUNE2016
DOIs
StatePublished - Jun 10 2016

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'A lipoprotein/b-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane'. Together they form a unique fingerprint.

  • Cite this