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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Nishiyama K,Maeda M,Yanagisawa K,Nagase R,Komura H,Iwashita T,Yamagaki T,Kusumoto S,Tokuda H,Shimamoto Kdoi
10.1038/ncomms2267subject
Has Abstractpub_date
2012-01-01 00:00:00pages
1260issn
2041-1723pii
ncomms2267journal_volume
3pub_type
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