Functional insight into the role of Orc6 in septin complex filament formation in Drosophila
| Autor: | Katarina Akhmetova, Maxim Balasov, Igor Chesnokov, Richard P. H. Huijbregts |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Cytoplasm
Genotype Protein subunit Origin Recognition Complex macromolecular substances Biology Septin ORC6 Cell cortex Fluorescence Resonance Energy Transfer Animals Drosophila Proteins Septin complex Molecular Biology Cytoskeleton Cytokinesis Hydrolysis fungi Cell Cycle Cell Biology Articles 3. Good health Cell biology Microscopy Electron Mutation Origin recognition complex Drosophila biological phenomena cell phenomena and immunity Protein Multimerization Drosophila Protein Septins Signal Transduction |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | Detailed roles of conserved septin motifs, GTP, and Orc6 in Drosophila septin complex functions are examined both in vitro and in vivo in a live animal. A novel mechanism of Orc6 regulation of septin filament formation is presented. Septins belong to a family of polymerizing GTP-binding proteins that are important for cytokinesis and other processes that involve spatial organization of the cell cortex. We reconstituted a recombinant Drosophila septin complex and compared activities of the wild-type and several mutant septin complex variants both in vitro and in vivo. We show that Drosophila septin complex functions depend on the intact GTP-binding and/or hydrolysis domains of Pnut, Sep1, and Sep2. The presence of the functional C-terminal domain of septins is required for the integrity of the complex. Drosophila Orc6 protein, the smallest subunit of the origin recognition complex (ORC), directly binds to septin complex and facilitates septin filament formation. Orc6 forms dimers through the interactions of its N-terminal, TFIIB-like domains. This ability of the protein suggests a direct bridging role for Orc6 in stimulating septin polymerization in Drosophila. Studies reported here provide a functional dissection of a Drosophila septin complex and highlight the basic conserved and divergent features among metazoan septin complexes. |
| Databáze: | OpenAIRE |
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