Isotypes of multilocalizing proteins from the cytoskeleton and their roles in differentiation and growth of pea seedlings.
| Project/Area Number |
16570034
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
植物生理・分子
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| Research Institution | Ehime University |
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Principal Investigator |
ABE Shunnosuke Ehime University, Faculty of Agriculture, professor, 農学部, 教授 (40167937)
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| Project Period (FY) |
2004 – 2006
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| Project Status |
Completed (Fiscal Year 2006)
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| Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2006: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2005: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2004: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | apyrase / Tudor / differentiation / Lateral root formation / sub-cellular localization / immunohistochemistry / translation / cytoskeleton / 4SNc-Tudor / 発芽 / マメ類 / 誘導酵素 / アピラーゼ / SN4TDR / 吸水 / 遺伝子発現 / タンパク質 / 分裂酵母 |
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| Research Abstract |
Expression, localization, and molecular structure of the heparin binding protein SN4TDR and apy1 from the pea cytoskeleton were studied. Both SN4TDR and apy1 were localized in the cytoplasm in pea seedling tissues and also induced in the primodium for lateral root formation. In some active cells, apy1 was also localized in nuclei. However, expression of SN4TDR was induced during imbibition and kept constant after germination as in tub1, while apy1 was induced 16 h after germination. Localization of these proteins in the cytoplasm were proved by immunohistochemistry in pea seedlings. When with the full SN4TDR was fused with XFP and expressed in S.pombe, the protein was proved to localize in cytoplasm, leaving nuclei unstained throughout the life cycle (vegetative, mating, and sporulation. Deletion experiments of the YFP construct in S.pombe implied the presence of nuclear exclusion signal (NES) with less than 50 aa long in SN4TDR. Yeast two hybridization followed by immunoprecipitation.proposed the tubulin binding subunit of translation initiation factor, moe1 and ribosomal protein L22 potent as candidates for association of SN4TDR in vivo. Phosphorylation of apy1 was also proved.
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Report
(4 results)
Research Products
(17 results)
