Stepwise Assembly of Dimeric F1Fo-ATP Synthase in Mitochondria Involves the Small Fo-Subunits k and i
| Autor: | Christiane D. Fichter, Martin van der Laan, Inge Perschil, Karina Wagner |
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| Rok vydání: | 2010 |
| Předmět: |
Electrophoresis
Cell Physiology Saccharomyces cerevisiae Proteins Mitochondrial intermembrane space ATPase Immunoblotting ATP synthase gamma subunit V-ATPase Molecular Biology Adenosine Triphosphatases biology ATP synthase Chemiosmosis Articles Cell Biology Mitochondrial Proton-Translocating ATPases Electron transport chain Mitochondria Proton-Translocating ATPases Biochemistry Mutation biology.protein Electrophoresis Polyacrylamide Gel Protein Multimerization Gene Deletion ATP synthase alpha/beta subunits |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e09-12-1023 |
| Popis: | Oligomerization of F1Fo-ATP synthase in the inner mitochondrial membrane governs the formation of cristae membrane domains. We show that the F1Fo-subunits Su i and Su k are crucial for the formation and maturation of ATP synthase dimers and oligomers. Su i additionally facilitates the incorporation of new subunits into ATP synthase monomers. F1Fo-ATP synthase is a key enzyme of oxidative phosphorylation that is localized in the inner membrane of mitochondria. It uses the energy stored in the proton gradient across the inner mitochondrial membrane to catalyze the synthesis of ATP from ADP and phosphate. Dimeric and higher oligomeric forms of ATP synthase have been observed in mitochondria from various organisms. Oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part. Several subunits were mapped to monomer-monomer-interfaces of yeast ATP synthase complexes, but only Su e (Atp21) and Su g (Atp20) have so far been identified as crucial for the formation of stable dimers. We show that two other small Fo-components, Su k (Atp19) and Su i (Atp18) are involved in the stepwise assembly of F1Fo-ATP synthase dimers and oligomers. We have identified an intermediate form of the ATP synthase dimer, which accumulates in the absence of Su i. Moreover, our data indicate that Su i facilitates the incorporation of newly synthesized subunits into ATP synthase complexes. |
| Databáze: | OpenAIRE |
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