MPIase is a glycolipozyme essential for membrane protein integration

Ken-ichi Nishiyama (), Masahide Maeda, Kayo Yanagisawa, Ryohei Nagase, Hajime Komura, Takashi Iwashita, Tohru Yamagaki, Shoichi Kusumoto, Hajime Tokuda and Keiko Shimamoto ()
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Ken-ichi Nishiyama: Cryobiofrontier Research Center, Faculty of Agriculture, Iwate University
Masahide Maeda: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Kayo Yanagisawa: Cryobiofrontier Research Center, Faculty of Agriculture, Iwate University
Ryohei Nagase: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Hajime Komura: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Takashi Iwashita: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Tohru Yamagaki: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Shoichi Kusumoto: Bioorganic Research Institute, Suntory Foundation for Life Sciences
Hajime Tokuda: Faculty of Nutritional Sciences, The University of Morioka
Keiko Shimamoto: Bioorganic Research Institute, Suntory Foundation for Life Sciences

Nature Communications, 2012, vol. 3, issue 1, 1-10

Abstract: Abstract Protein integration into biological membranes is a vital cellular event for all organisms. We previously reported an integration factor in the inner membrane of Escherichia coli, named MPIase (membrane protein integrase). Here we show that in contrast to previously identified integration factors that are proteins, MPIase is a glycolipid composed of diacylglycerol and a glycan chain of three acetylated aminosugars linked through pyrophosphate. Hydrolytic removal of the lipid moiety gives a soluble product with higher integration activity than that of the original MPIase. This soluble form of MPIase directly interacts with a newborn membrane protein, maintaining its integration-competent structure and allowing its post-translational integration. MPIase actively drives protein integration following chaperoning membrane proteins. We further demonstrate with anti-MPIase antibodies that MPIase is likely involved in integration in vivo. Collectively, our results suggest that MPIase, essential for membrane protein integration, is to our knowledge the first glycolipid with an enzyme-like activity.

Date: 2012
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DOI: 10.1038/ncomms2267

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