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Elife. 2016 Jun 10;5. pii: e15276. doi: 10.7554/eLife.15276.

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

Author information

1
Department of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United States.

Abstract

Lipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with β-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.

KEYWORDS:

Bam complex; CAMP; E. coli; infectious disease; membrane biogenesis; microbiology; polymyxin B; signal transduction; surface exposed lipoprotein

PMID:
27282389
PMCID:
PMC4942254
DOI:
10.7554/eLife.15276
[Indexed for MEDLINE]
Free PMC Article

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