| Project/Area Number |
11460155
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Mie University |
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Principal Investigator |
HATTORI Tsukaho Mie University, Center for Molecular Biology and Genetics, Associate Professor, 遺伝子実験施設, 助教授 (10164865)
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| Co-Investigator(Kenkyū-buntansha) |
TOYODA Akiko (YAMANOTO Akiko) Mie University, Center for Molecular Biology and Genetics, Assistant Professor, 遺伝子実験施設, 助手 (70263027)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥15,200,000 (Direct Cost: ¥15,200,000)
Fiscal Year 2001: ¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2000: ¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 1999: ¥9,100,000 (Direct Cost: ¥9,100,000)
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| Keywords | absicisic acid / TRAB1 / rice (Oryza sativa) / phosphorylation / signal transduction / ABA / 転写因子 / イネ(Oryza sativa) / bZIP型タンパク質 / GAL4 / VP1 / 酵母 |
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| Research Abstract |
The rice basic region-leucine zipper (bZIP) factor TRAB1 binds to abscisic acid response elements (ABREs) and mediates abscisic acid (ABA) signals to activate transcription. We show here that TRAB1is rapidly phosphorylated by in vivo labeling experiments and by phosphatase-sensitive mobilty-shifts on a SDS-polyacrylamide gel. We previously have shown that a chimeric promoter containing GAL4-binding sites becomes ABA-inducible when a GAL4-binding domain : : TRAB1 fusion protein is expressed. This expression system allowed us to assay the ABA-response function of TRAB1. Using this assay system, we have identified that Ser-44 of TRAB1 is critical for this function. Since ABA-induced mobility-shift was not observed when Ser-44 was mutated to alanine, this serine residue is suggested to be phosphorylated in response to ABA. Cell-fractionation experiments as well as the fluorescent microscopic observation of transiently expressed GFP : : TRAB1 fusion protein indicated that TRAB1 is localized in the nucleus independently of ABA. Our results suggest that the end or near-end point event of the primary ABA signal transduction pathway is the phosphorylation in the nucleus of pre-existing TRAB1 and probablly other homologous ABRE -binding factors.
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