Novel Glycolipid Involved in Membrane Protein Integration: Structure and Mode of Action

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  • Fujikawa Kohki
    Bioorganic Research Institute, Suntory Foundation for Life Sciences
  • Nomura Kaoru
    Bioorganic Research Institute, Suntory Foundation for Life Sciences
  • Nishiyama Ken-ichi
    Department of Biological Chemistry, Faculty of Agriculture, Iwate University
  • Shimamoto Keiko
    Bioorganic Research Institute, Suntory Foundation for Life Sciences

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Abstract

<p>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.</p>

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