Journal of Synthetic Organic Chemistry, Japan
Online ISSN : 1883-6526
Print ISSN : 0037-9980
ISSN-L : 0037-9980
Accounts
Novel Glycolipid Involved in Membrane Protein Integration: Structure and Mode of Action
Kohki FujikawaKaoru NomuraKen-ichi NishiyamaKeiko Shimamoto
Author information
JOURNALS OPEN ACCESS

2019 Volume 77 Issue 11 Pages 1096-1105

Details
Abstract

Membrane protein integration is a vital event in cells. We identified a novel factor involved in this process in Escherichia coli, which we named MPIase after its function. A combination of spectroscopic analyses and synthetic work has revealed that MPIase is a glycolipid despite its enzyme-like activity. MPIase has a long glycan chain composed of repeating trisaccharide units and an anchor composed of a pyrophosphate and a diacylglycerol. To determine the mechanism of activity, we synthesized a trisaccharyl pyrophospholipid termed mini-MPIase-3, a minimal unit of MPIase, and its derivatives. Structure-activity relationship studies demonstrated that the glycan part of MPIase prevents the aggregation of substrate proteins. Moreover, MPIase embedded in the membrane alters the physicochemical properties of membranes to facilitate proteins to interact with the inner part of the membrane.

Information related to the author
© 2019 The Society of Synthetic Organic Chemistry, Japan
Previous article Next article
feedback
Top