Regulation of Arabidopsis life cycle by the hsp 70 system of the endoplasmic reticulum
| Project/Area Number |
15570034
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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 | Nagoya University |
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Principal Investigator |
NISHIKAWA Shuh-ichi Nagoya University, Graduate School of Science, Associate Professor, 大学院・理学研究科, 助教授 (10252222)
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| Project Period (FY) |
2003 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2004: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2003: ¥2,400,000 (Direct Cost: ¥2,400,000)
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| Keywords | endoplasmic reticulum / quality control / molecular chaperone / hsp 70 / Arabidopsis thaliana / pollen / 小胞体 / DnaJホモログ / BiP |
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| Research Abstract |
The endoplasmic reticulum(ER) is the entrance of the secretory pathway in eukaryotic cells. Secretory and membrane proteins undergo folding and various modification processes before they are exported to the Golgi apparatus. Quality control mechanisms in the ER monitor these processes to ensure that defective proteins that failed to acquire correct functional structures are not deployed throughout the cells and play important roles in the maintenance of cell homeostasis. The aim of our research is to elucidate functions and mechanisms of the ER quality control system in plant development by analyzing functions of molecular chaperones in the ER, molecular machineries that control ER quality control. BiP, a Hsp 70 family molecular chaperone in the ER, plays a central role both in protein translocation across the ER membrane and ER quality control. In this study, we have developed a system to analyze BiP functions in plant cells using Arabidopsis thaliana.
In order to compromise BiP functions in plant cells, we introduced a series of dominant negative mutations into the Arabidopsis BIP gene. When expressed one of the dominant negative mutants in the Arabidopsis culture cells using the 35S promoter, we observed change of subcellular distribution of 12S globulin-GFP fusion protein which can be attributed to its aggregation. We also constructed transgenic plants which express BiP mutants in pollen under the LAT52 promoter. Reciprocal cross experiments suggested that expression of BiP mutants caused pollen sterility. Analyses of yeast mutants identified three J-domain containing protein in the ER as partners for BiP during its function. We identified Arabidopsis homologues of yeast J-domain containing proteins in the ER and constructed their T-DNA insertion mutants.
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Report
(3 results)
Research Products
(20 results)
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[Journal Article] Re-investigation of the requirement of cytosolic ATP for mitochondrial protein import.2004
Author(s)
Asai, T., Takahashi, T., Esaki, M., Nishikawa, S., Ohtsuka, K., Nakai, M., Endo, T.
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Journal Title
J.Biol.Chem. 279
Pages: 19464-19470
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Mitochondrial protein import : Requirement of the presequence elements and TOM components for precursor binding to the TOM complex.2004
Author(s)
Esaki, M., Shimizu, H., Ono, T., Yamamoto, H., Kanamori, T., Nishikawa, S., Endo, T.
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Journal Title
J.Biol.Chem. 279
Pages: 45701-45707
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space.2004
Author(s)
Naoe, M., Ohwa, Y, Ishikawa, D., Ohshima, C., Nishikawa, S., Yamamoto, H., Endo, T.
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Journal Title
J.Biol.Chem. 279
Pages: 47815-17821
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast.2004
Author(s)
Nakatsukasa, K., Okada, S., Umebayashi, K., Fukuda, R., Nishikawa, S., Endo, T.
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Journal Title
J.Biol.Chem. 279
Pages: 49762-49772
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion.2003
Author(s)
Nishikawa, S., Terazawa, Y., Nakayama, T., Hirata, A., Makio, T., Endo, T.
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Journal Title
J.Biol.Chem. 278
Pages: 9938-9943
Description
「研究成果報告書概要(欧文)」より
Related Report
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[Journal Article] Tom40 protein import channel binds to non-native proteins and prevents their aggregation.2003
Author(s)
Esaki, M., Kanamori, T., Nishikawa, S., Shin, I., Schultz, P.G., Endo, T.
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Journal Title
Nat.Struct.Biol. 10
Pages: 988-994
Description
「研究成果報告書概要(欧文)」より
Related Report
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