Ring assembly of c subunits of F0F1 ‐ATP synthase in Propionigenium modestum requires YidC and UncI following MPIase‐dependent membrane insertion

AbstractThe c subunits of F0F1‐ATP synthase (F0c) 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 ofPropionigenium modestum F0c (Pm ‐F0c), of which the ring structure is resistant to SDS. Ring assembly of Pm ‐F0c requiresP. modestum UncI (Pm ‐UncI). Ring assembly ofin vitro synthesized Pm ‐F0c was observed when both YidC and Pm ‐UncI were reconstituted into liposomes ofE. coli phospholipids. Under the physiological conditions where spontaneous insertion had been blocked by diacylglycerol, MPIase was necessary for Pm ‐F0c 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‐F0c.

Source: FEBS Letters - January 10, 2021 Category: Biochemistry Authors: Hanako Nishikawa, Kotoka Kanno, Yuta Endo, Ken ‐ichi Nishiyama Tags: RESEARCH LETTER Source Type: research