Journal
SCIENCE ADVANCES
Volume 8, Issue 38, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abq8303
Keywords
-
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [263531414]
- Sigrid Juselius Foundation
- Ruth and Nils-Erik Stenback's Foundation
- Magnus Ehrnrooth Foundation
Ask authors/readers for more resources
Rhomboid proteins regulate membrane thickness to accommodate specific functions. The activity of GlpG protease is influenced by the lipid environment, showing no lipid headgroup specificity.
Membrane thinning by rhomboid proteins has been proposed to reduce hydrophobic mismatch, providing a unique environment for important functions ranging from intramembrane proteolysis to retrotranslocation in protein degradation. We show by in vitro reconstitution and solid-state nuclear magnetic resonance that the lipid environment of the Escherichia coli rhomboid protease GlpG influences its activity with an optimal hydrophobic membrane thickness between 24 and 26 angstrom. While phosphatidylcholine membranes are only negligibly altered by GlpG, in an E. coli-relevant lipid mix of phosphatidylethanolamine and phosphatidylglycerol, a thinning by 1.1 angstrom per leaflet is observed. Protease activity is strongly correlated with membrane thickness and shows no lipid headgroup specificity. We infer from these results that, by adjusting the thickness of specific membrane domains, membrane proteins shape the bilayer for their specific needs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available