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Mitochondrial ATP synthasome: Expression and structural interaction of its components
H. Nůsková, T. Mráček, T. Mikulová, M. Vrbacký, N. Kovářová, J. Kovalčíková, P. Pecina, J. Houštěk,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adenosine Triphosphate biosynthesis MeSH
- Fibroblasts metabolism MeSH
- Phosphates chemistry metabolism MeSH
- Rats MeSH
- Cells, Cultured MeSH
- Humans MeSH
- Macromolecular Substances chemistry metabolism MeSH
- Mitochondrial ADP, ATP Translocases chemistry genetics metabolism MeSH
- Mitochondrial Proton-Translocating ATPases chemistry genetics metabolism MeSH
- Mitochondria metabolism MeSH
- Animals, Newborn MeSH
- Rats, Wistar MeSH
- Mitochondria, Heart metabolism MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Mitochondrial ATP synthase, ADP/ATP translocase (ANT), and inorganic phosphate carrier (PiC) are supposed to form a supercomplex called ATP synthasome. Our protein and transcript analysis of rat tissues indicates that the expression of ANT and PiC is transcriptionally controlled in accordance with the biogenesis of ATP synthase. In contrast, the content of ANT and PiC is increased in ATP synthase deficient patients' fibroblasts, likely due to a post-transcriptional adaptive mechanism. A structural analysis of rat heart mitochondria by immunoprecipitation, blue native/SDS electrophoresis, immunodetection and MS analysis revealed the presence of ATP synthasome. However, the majority of PiC and especially ANT did not associate with ATP synthase, suggesting that most of PiC, ANT and ATP synthase exist as separate entities.
References provided by Crossref.org
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