Ring assembly of c subunits of F 0 F 1 -ATP synthase in Propionigenium modestum requires YidC and UncI following MPIase-dependent membrane insertion

FEBS Letters

article

Hanako Nishikawa¹  Kotoka Kanno²  Yuta Endo¹  Ken-ichi Nishiyama¹ 

[1] The United Graduate School of Agricultural Sciences, Iwate University;Department of Biological Chemistry and Food Science, Faculty of Agriculture, Iwate University

关键词: F0c ring assembly;    membrane protein insertion;    MPIase;    Propionigenium modestum;    UncI;    YidC;   

DOI  :  10.1002/1873-3468.14036

来源: John Wiley & Sons Ltd.

【 摘 要 】

The c subunits of F 0 F 1 -ATP synthase (F 0 c) assemble into a ring structure, following membrane insertion that is dependent on both glycolipid MPIase and protein YidC. We analyzed the insertion and assembly processes of Propionigenium modestum F 0 c (Pm-F 0 c), of which the ring structure is resistant to SDS. Ring assembly of Pm-F 0 c requires P. modestum UncI (Pm-UncI). Ring assembly of in vitro synthesized Pm-F 0 c was observed when both YidC and Pm-UncI were reconstituted into liposomes of Escherichia coli phospholipids. Under the physiological conditions where spontaneous insertion had been blocked by diacylglycerol, MPIase was necessary for Pm-F 0 c insertion allowing the subsequent YidC/Pm-UncI-dependent ring assembly. Thus, we have succeeded in the complete reconstitution of membrane insertion and subsequent ring assembly of Pm-F 0 c.

【 授权许可】

Unknown