Isolation of a Novel 190 kDa Protein from Tobacco BY-2 Cells: Possible Involvement in the Interaction between Actin Filaments and Microtubules
| Autor: | Hitoshi Mori, Teruo Shimmen, Hidefumi Orii, Hisako Igarashi, Seiji Sonobe |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Tobacco BY-2 cells
Cell division Physiology Molecular Sequence Data Arp2/3 complex Plant Science Microfilament Phragmoplast Microtubules Tobacco Amino Acid Sequence Cloning Molecular Cytoskeleton Actin Plant Proteins Base Sequence biology Actin remodeling Cell Biology General Medicine Cell biology Actin Cytoskeleton Plants Toxic Biochemistry biology.protein Microtubule-Associated Proteins Protein Binding |
| Zdroj: | Plant and Cell Physiology. 41:920-931 |
| ISSN: | 1471-9053 0032-0781 |
| DOI: | 10.1093/pcp/pcd015 |
| Popis: | Interaction between actin filaments (AFs) and microtubules (MTs) has been reported in various plant cells, and the presence of a factor(s) connecting these two cytoskeletal networks has been suggested, but its molecular entity has not been elucidated yet. We obtained a fraction containing MT-binding polypeptides, which induced bundling of AFs and of MTs. A 190 kDa polypeptide which associated with AFs was selectively isolated from the fraction. This polypeptide was thought to have an ability to bind to both AFs and MTs. We raised a monoclonal antibody against the 190 kDa polypeptide. Immunostaining demonstrated the association of the 190 kDa polypeptide with AF bundles and with MT bundles formed in vitro. Immunocytochemical studies throughout the cell cycle revealed that the 190 kDa polypeptide was localized in the nucleus before nuclear envelope breakdown, and in the spindle and the phragmoplast during cell division. After the re-formation of the nuclear envelope, the 190 kDa polypeptide was sequestered to the daughter nuclei. Using the antibody, we succeeded in cloning a cDNA encoding the 190 kDa polypeptide. |
| Databáze: | OpenAIRE |
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