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 |