Reconstitution of the initial steps of mitochondrial protein import
| Autor: | Katsuyoshi Mihara, Kitaru Suda, Gottfried Schatz, Martin Horst, Trevor Lithgow, Naomi Hachiya |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Receptors Cytoplasmic and Nuclear Receptors Cell Surface Saccharomyces cerevisiae Mitochondrion Mitochondrial Membrane Transport Proteins Fungal Proteins Mitochondrial membrane transport protein Mitochondrial Precursor Protein Import Complex Proteins Protein Precursors Adenosine Triphosphatases Signal recognition particle Multidisciplinary biology Endoplasmic reticulum Adrenodoxin Membrane Proteins Membrane Transport Proteins Membrane transport Mitochondria Cytosol 14-3-3 Proteins Biochemistry Chaperone (protein) biology.protein Bacterial outer membrane Molecular Chaperones |
| Zdroj: | Nature. 376:705-709 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/376705a0 |
| Popis: | We have reconstituted the initial steps of mitochondrial protein import with a purified precursor protein, a purified, ATP-dependent, cytosolic chaperone selective for mitochondrial precursors (mitochondrial import stimulating factor; MSF), and either intact mitochondria or intact or solubilized mitochondrial outer membranes. We show that the precursor-MSF complex first binds to the Mas37p/Mas70p subunits of the mitochondrial import receptor. After ATP-dependent release of MSF, the precursor is transferred from Mas37p/Mas70p to the Mas20p/Mas22p subunits of the receptor, and finally delivered to the import channel in the outer membrane. Import in the absence of the MSF bypasses Mas37p/Mas70p. The ATP-mediated transfer of a precursor from MSF to specific subunits of the import receptor is similar to the GTP-mediated transfer of precursors from the signal recognition particle to its receptor on the endoplasmic reticulum. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|