2000 Fiscal Year Final Research Report Summary
Multiple functions of elongation factor 1
Project/Area Number |
11460033
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Research Category |
Grant-in-Aid for Scientific Research (B).
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
応用微生物学・応用生物化学
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Research Institution | Iwate University |
Principal Investigator |
EJIRI Shin-ichiro Department of Agriculture, Iwate University Professor, 農学部, 教授 (90005629)
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Co-Investigator(Kenkyū-buntansha) |
KIDOU Shin-ichiro Department of Agriculture, Iwate University Associate Professor, 農学部, 助教授 (60271847)
|
Project Period (FY) |
1999 – 2000
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Keywords | elongation factor / EF-1 / glutathion S-transferase / actin filament |
Research Abstract |
Elongation factor EF-1 consists of four subunits (EF-1 αββ'γ). EF-1α・GTP catalyzes the binding of aminoacyl-tRNA to the ribosome. EF-1β and EF-1β' catalyze the GOP/GTP exchange on EF-1α・GDP, However, the function of EF-1γ, a subunit detected in eukaryotes, but not in prokaryotes remained unknown. In this studies we demonstrated that rice EF-1ββ'γ and recombinant EF-1γ possess glutathione Stransferase (GST) activity. The EF-1ββ'γ-or EF-1γ- dependent GST activity is about one-fiftieth of the rice GST activity. This is the first indication of glutathione Stransferase activity in EF-1γ. Moreover, we demonstrated that EF-1α-GFP and EF1γ-GFP are co-localized with actin filaments in the cytoplasm of tobacco BY-2 cell at interphase. Surprisingly, both fusion proteins are located on spindle bodies at the stage of nuclear fission. As moonlighting functions of EF-1, such as cytoskeietal organization, apoptosis, and oncogenic transformation. have been reported, our results will facilitate the understanding of the underlying molecular mechanisms of these processes.
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Research Products
(6 results)
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[Publications] Kamiie, K., Nomura, Y., Kobayashi, S., Taira, H., Kobayashi, K., Matsuzawa, H., Yamashita, T., Kidou, S.and Ejiri, S.: "Cloning and expression of silk gland elongation factor 1γ in Escherichia coli."Biosci. Biotech. Biochem.. (in press). (2002)
Description
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