The Mitochondrial Receptor Complex: the Small Subunit Mom8b/Isp6 Supports Association of Receptors with the General Insertion Pore and Transfer of Preproteins
| Autor: | Angelika Hönlinger, M Moczko, Agustin Alconada, Nikolaus Pfanner, M Kübrich |
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| Rok vydání: | 1995 |
| Předmět: |
Receptor complex
Saccharomyces cerevisiae Proteins Macromolecular Substances Saccharomyces cerevisiae Receptors Cytoplasmic and Nuclear Cooperativity TIM/TOM complex Biology Mitochondrial Membrane Transport Proteins Fungal Proteins Mitochondrial Precursor Protein Import Complex Proteins Receptor Molecular Biology Sorting and assembly machinery Preprotein binding Membrane Proteins Biological Transport Intracellular Membranes Cell Biology biology.organism_classification Cell Compartmentation Mitochondria Cell biology Bacterial outer membrane Protein Processing Post-Translational Gene Deletion Research Article |
| Zdroj: | Molecular and Cellular Biology. 15:6196-6205 |
| ISSN: | 1098-5549 |
| Popis: | The mitochondrial outer membrane contains import receptors for preproteins and a multisubunit general insertion pore. Several small outer membrane proteins (< 10 kDa) have been identified by their association with receptors or the general insertion pore, yet little is known about their function. Here, we present evidence that the biochemically identified Mom8b and the genetically identified Isp6 are identical. A deletion of Mom8b/Isp6 in Saccharomyces cerevisiae leads to (i) a delay of import of preproteins, (ii) stabilization of preprotein binding to receptors and the general insertion pore, and (iii) destabilization of the interaction between receptors and the general insertion pore. These results suggest that Mom8b supports the cooperativity between receptors and the general insertion pore and facilitates the release of preproteins from import components and thereby promotes efficient transfer of preproteins. |
| Databáze: | OpenAIRE |
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