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Membrane remodeling capacity of a vesicle-inducing glycosyltransferase
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2014 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 281, no 16, 3667-3684 p.Article in journal (Refereed) Published
Abstract [en]

Intracellular vesicles are abundant in eukaryotic cells but absent in the Gram-negative bacterium Escherichia coli. However, strong overexpression of a monotopic glycolipid-synthesizing enzyme, monoglucosyldiacylglycerol synthase from Acholeplasma laidlawii (alMGS), leads to massive formation of vesicles in the cytoplasm of E. coli. More importantly, alMGS provides a model system for the regulation of membrane properties by membrane-bound enzymes, which is critical for maintaining cellular integrity. Both phenomena depend on how alMGS binds to cell membranes, which is not well understood. Here, we carry out a comprehensive investigation of the membrane binding of alMGS by combining bioinformatics methods with extensive biochemical studies, structural modeling and molecular dynamics simulations. We find that alMGS binds to the membrane in a fairly upright manner, mainly by residues in the N-terminal domain, and in a way that induces local enrichment of anionic lipids and a local curvature deformation. Furthermore, several alMGS variants resulting from substitution of residues in the membrane anchoring segment are still able to generate vesicles, regardless of enzymatic activity. These results clarify earlier theories about the driving forces for vesicle formation, and shed new light on the membrane binding properties and enzymatic mechanism of alMGS and related monotopic GT-B fold glycosyltransferases.

Place, publisher, year, edition, pages
2014. Vol. 281, no 16, 3667-3684 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-232517DOI: 10.1111/febs.12889PubMedID: 24961908OAI: oai:DiVA.org:uu-232517DiVA: diva2:748490
Swedish National Infrastructure for Computing (SNIC), SNIC 2013/1-202
Available from: 2014-09-19 Created: 2014-09-19 Last updated: 2016-06-16

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Lindén, Martin
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