The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit δ
| Autor: | Matthieu J. Caron, Marie-France Giraud, Jean-Paul di Rago, Jean Velours, Stéphane Duvezin-Caubet |
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| Rok vydání: | 2003 |
| Předmět: |
Time Factors
Protein Conformation Protein subunit Saccharomyces cerevisiae Mitochondrion Mitochondrial Proton-Translocating ATPases Catalysis Cell membrane Oxygen Consumption Protein structure ATP synthase gamma subunit Escherichia coli medicine Inner membrane Promoter Regions Genetic Adenosine Triphosphatases Multidisciplinary biology Hydrolysis Cell Membrane Biological Sciences biology.organism_classification Mitochondria Protein Structure Tertiary Proton-Translocating ATPases medicine.anatomical_structure Microscopy Fluorescence Biochemistry Doxycycline Biophysics biology.protein Electrophoresis Polyacrylamide Gel |
| Zdroj: | Proceedings of the National Academy of Sciences. 100:13235-13240 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | The mitochondrial ATP synthase is made of a membrane-integrated F 0 component that forms a proton-permeable pore through the inner membrane and a globular peripheral F 1 domain where ATP is synthesized. The catalytic mechanism is thought to involve the rotation of a 10-12 c subunit ring in the F 0 together with the γ subunit of F 1 . An important and not yet resolved question is to define precisely how the γ subunit is connected with the c -ring. In this study, using a doxycycline-regulatable expression system, we provide direct evidence that the rest of the enzyme can assemble without the δ subunit of F 1 , and we show that δ-less mitochondria are uncoupled because of an F 0 -mediated proton leak. Based on these observations, and taking into account high-resolution structural models, we propose that subunit δ plays a key role in the mechanical coupling of the c -ring to subunit γ. |
| Databáze: | OpenAIRE |
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