Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane
| العنوان: | Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane |
|---|---|
| المؤلفون: | Patrick D'Silva, Qinglian Liu, William Walter, Elizabeth A. Craig |
| المصدر: | Nature Structural & Molecular Biology. 11:1084-1091 |
| بيانات النشر: | Springer Science and Business Media LLC, 2004. |
| سنة النشر: | 2004 |
| مصطلحات موضوعية: | Models, Molecular, Saccharomyces cerevisiae Proteins, Time Factors, Protein Conformation, Translocase of the outer membrane, Saccharomyces cerevisiae, Biology, Mitochondrial Membrane Transport Proteins, Mitochondrial membrane transport protein, Adenosine Triphosphate, Structural Biology, Mitochondrial Precursor Protein Import Complex Proteins, Escherichia coli, Immunoprecipitation, HSP70 Heat-Shock Proteins, Inner mitochondrial membrane, Molecular Biology, Gene Library, Adenosine Triphosphatases, Dose-Response Relationship, Drug, Hydrolysis, Peripheral membrane protein, Biological Transport, Intracellular Membranes, Mitochondrial carrier, Translocon, Mitochondria, Protein Structure, Tertiary, Cell biology, Protein Transport, Spectrometry, Fluorescence, Mutation, Translocase of the inner membrane, biology.protein, Anisotropy, ATP–ADP translocase, Peptides, Plasmids, Protein Binding |
| الوصف: | Preproteins synthesized on cytosolic ribosomes, but destined for the mitochondrial matrix, pass through the presequence translocase of the inner membrane. Translocation is driven by the import motor, having at its core the essential chaperone mtHsp70 (Ssc1 in yeast). MtHsp70 is tethered to the translocon channel at the matrix side of the inner membrane by the peripheral membrane protein Tim44. A key question in mitochondrial import is how the mtHsp70-Tim44 interaction is regulated. Here we report that Tim44 interacts with both the ATPase and peptide-binding domains of mtHsp70. Disruption of these interactions upon binding of polypeptide substrates requires concerted conformational changes involving both domains of mtHsp70. Our results fit a model in which regulated interactions between Tim44 and mtHsp70, controlled by polypeptide binding, are required for efficient translocation across the mitochondrial inner membrane in vivo. |
| تدمد: | 1545-9985 1545-9993 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dc8711c1481503e378bc6025a28e1a1Test https://doi.org/10.1038/nsmb846Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....2dc8711c1481503e378bc6025a28e1a1 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15459985 15459993 |
|---|