Role of MINOS in Mitochondrial Membrane Architecture
| Autor: | Thomas Becker, Ida J. van der Klei, Ralf M. Zerbes, Anita M. Kram, Silke Oeljeklaus, Karina von der Malsburg, Martin van der Laan, Nils Wiedemann, Nikolaus Pfanner, Marten Veenhuis, Maria Bohnert, Bettina Warscheid, David A. Stroud |
|---|---|
| Přispěvatelé: | Molecular Cell Biology |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
MINOS1
Saccharomyces cerevisiae Proteins SAM complex Mitochondrial intermembrane space Translocase of the outer membrane BIOGENESIS Saccharomyces cerevisiae ORGANIZATION Biology Mitochondrial Membrane Transport Proteins MECHANISMS Mitochondrial Proteins Mitochondrial membrane transport protein FUSION Structural Biology PROTEIN-IMPORT INNER-MEMBRANE Inner mitochondrial membrane Molecular Biology Sorting and assembly machinery Fcj1 COMPLEX MICOS complex ATP SYNTHASE INTERMEMBRANE SPACE Membrane Proteins Cell biology Mitochondria Protein Structure Tertiary Protein Transport Mio10 Translocase of the inner membrane Mitochondrial Membranes biology.protein Intermembrane space PROHIBITINS |
| Zdroj: | Journal of Molecular Biology, 422(2), 183-191. Academic Press |
| ISSN: | 0022-2836 |
| Popis: | The mitochondrial inner membrane contains a large protein complex crucial for membrane architecture, the mitochondrial inner membrane organizing system (MINOS). MINOS is required for keeping cristae membranes attached to the inner boundary membrane via crista junctions and interacts with protein complexes of the mitochondrial outer membrane. To study if outer membrane interactions and maintenance of cristae morphology are directly coupled, we generated mutant forms of mitofilin/Fcj1 (formation of crista junction protein 1), a core component of MINOS. Mitofilin consists of a transmembrane anchor in the inner membrane and intermembrane space domains, including a coiled-coil domain and a conserved C-terminal domain. Deletion of the C-terminal domain disrupted the MINOS complex and led to release of cristae membranes from the inner boundary membrane, whereas the interaction of mitofilin with the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM) were enhanced. Deletion of the coiled-coil domain also disturbed the MINOS complex and cristae morphology; however, the interactions of mitofilin with TOM and SAM were differentially affected. Finally, deletion of both intermembrane space domains disturbed MINOS integrity as well as interactions with TOM and SAM. Thus, the intermembrane space domains of mitofilin play distinct roles in interactions with outer membrane complexes and maintenance of MINOS and cristae morphology, demonstrating that MINOS contacts to TOM and SAM are not sufficient for the maintenance of inner membrane architecture. (C) 2012 Elsevier Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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