RRC ID 27310
著者 Nishiyama K, Maeda M, Yanagisawa K, Nagase R, Komura H, Iwashita T, Yamagaki T, Kusumoto S, Tokuda H, Shimamoto K.
タイトル MPIase is a glycolipozyme essential for membrane protein integration.
ジャーナル Nat Commun
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.
巻・号 3
ページ 1260
公開日 2012-1-1
DOI 10.1038/ncomms2267
PII ncomms2267
PMID 23232390
PMC PMC3535364
MeSH Escherichia coli / enzymology* Escherichia coli / metabolism Escherichia coli / physiology Glycolipids / chemistry Glycolipids / metabolism Glycolipids / physiology* Membrane Proteins / metabolism* Membrane Proteins / physiology Molecular Chaperones / metabolism Molecular Chaperones / physiology Protein Processing, Post-Translational / physiology Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Structure-Activity Relationship
IF 12.121
引用数 22
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
原核生物(大腸菌) Keio collection