| Project/Area Number |
17580005
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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 |
Breeding science
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| Research Institution | Kyoto University |
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Principal Investigator |
NAKAZAKI Tetsuya Kyoto University, Graduate School of Agriculture, Lecturer (60217693)
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| Co-Investigator(Kenkyū-buntansha) |
TANISAKA Takatoshi Kyoto University, Graduate School of Agriculture, Professor (80026591)
OKUMOTO Yutaka Kyoto University, Graduate School of Agriculture, Associate Professor (90152438)
HORIBATA Akira Kinki University, Faculty of Biology-Oriented Science, Lecturer (70258060)
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| Project Period (FY) |
2005 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,300,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2007: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2006: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2005: ¥900,000 (Direct Cost: ¥900,000)
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| Keywords | mPing / Transposon / Rurm 1 system / Rice / Mutant line IM294 / Rurmlシステム / RURM1システム |
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| Research Abstract |
Transposable activity of an active-transposon mPing in a rice mutant line, IM294 is much higher than in the original variety Gimbozu. Because IM294 is considered harboring a recessive mutation allele at Rurm1 locus, it is very likely that the destruction of the normal Rurm1 gene participates in high mPing transposable activity of IM294. We analyzed a change to occur by function loss of the Rurm1 gene to elucidate a novel rice protein conjugation system relating to the RURM1 protein (Rurm1 system), and this study was going to get the due to clarify the induction mechanism for the transposition of mPing.
At first in this study, we analyzed the influence that the function loss of Rurm1 gave transposition frequency of mPing using the transposon display method. As a result, high-frequency transposition of mPing relation to the function loss of Rum/ was confirmed in a various genetic background, and it was suggested that the function loss of Rurm1 was one of the causes to raise transposition frequency of mPing (preparing for submission). In addition, we successfully established the system to purifying RURM1 protein with bacterial recombinant protein expression system including detection of a culture condition to produce soluble non-denaturation RURM1 protein. Anti-RURM1 antibody was obtained with the purified recombinant RURM1 protein and the provided anti-RURM1 antibody confirmed specific recognition for RURM1 protein This anti-RURM1 antibody would be useful to identify proteins, which participate in a RURM1 protein conjugation system. Furthermore, in this study, a TOR (target of rapamycin) gene of the rice was identified and an expression analysis was performed. Then, it was found possibility that the protein conjugation system for RURM1 protein (urmylation) bears an essential role in the mechanism for controlling cell division in rice plant.
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