Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein
| Autor: | Akihiro Jofuku, Naotada Ishihara, Katsuyoshi Mihara |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
FIS1
endocrine system Molecular Sequence Data Biophysics Mitochondria Liver Biology Biochemistry Mitochondrial Proteins Structure-Activity Relationship Animals Humans Tissue Distribution Amino Acid Sequence Molecular Biology HSPA9 Cell Membrane Peripheral membrane protein Cell Biology Mitochondrial carrier Protein Structure Tertiary Rats Cell biology Molecular Weight Organ Specificity Translocase of the inner membrane Mutagenesis Site-Directed DNAJA3 Mitochondrial fission ATP–ADP translocase HeLa Cells |
| Zdroj: | Biochemical and Biophysical Research Communications. 333:650-659 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2005.05.154 |
| Popis: | In yeast, mitochondrial-fission is regulated by the cytosolic dynamin-like GTPase (Dnm1p) in conjunction with a peripheral protein, Mdv1p, and a C-tail-anchored outer membrane protein, Fis1p. In mammals, a dynamin-related protein (Drp1) and Fis1 are involved in the mitochondrial-fission reaction as Dnm1 and Fis1 orthologues, respectively. The involvement of other component(s), such as the Mdv1 homologue, and the mechanisms regulating mitochondrial-fission remain unclear. Here, we identified rat Fis1 (rFis1) and analyzed its structure-function relationship. Blue-native-polyacrylamide gel electrophoresis revealed that rFis1 formed a approximately 200-kDa complex in the outer mitochondrial membrane. Its expression in HeLa cells promoted extensive mitochondrial fragmentation, and gene knock-down by RNAi induced extension of the mitochondrial networks. Taking advantage of these properties, we analyzed functional domains of rFis1. These experiments revealed that the N-terminal and C-terminal segments are both essential for oligomeric rFis1 interaction, and the middle TPR-like domains regulate proper oligomer assembly. Any mutations that disturb the proper oligomeric assembly compromise mitochondrial division-stimulating activity of rFis1. |
| Databáze: | OpenAIRE |
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