Ring assembly of c subunits of F 0 F 1 ‐ATP synthase in Propionigenium modestum requires YidC and UncI following MPIase‐dependent membrane insertion
| Autor: | Kotoka Kanno, Ken-ichi Nishiyama, Hanako Nishikawa, Yuta Endo |
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| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
Liposome biology ATP synthase Chemistry 030302 biochemistry & molecular biology Biophysics Cell Biology Ring (chemistry) biology.organism_classification medicine.disease_cause Biochemistry Propionigenium modestum In vitro 03 medical and health sciences Glycolipid Structural Biology Genetics medicine biology.protein Molecular Biology Escherichia coli 030304 developmental biology Diacylglycerol kinase |
| Zdroj: | FEBS Letters. 595:647-654 |
| ISSN: | 1873-3468 0014-5793 |
| Popis: | The c subunits of F0 F1 -ATP synthase (F0 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 F0 c (Pm-F0 c), of which the ring structure is resistant to SDS. Ring assembly of Pm-F0 c requires P. modestum UncI (Pm-UncI). Ring assembly of in vitro synthesized Pm-F0 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-F0 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-F0 c. |
| Databáze: | OpenAIRE |
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