| Project/Area Number |
06454137
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
ISOGAI Akira Nara Institute of Science and Technology, Graduate School of Biological Sciences. Professor, バイオサイエンス研究科, 教授 (20011992)
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| Co-Investigator(Kenkyū-buntansha) |
CHE Fang-Sik Nara Institute of Science and Technology, Graduate School of Biological Sciences, バイオサイエンス研究科, 助手 (00263442)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥7,200,000 (Direct Cost: ¥7,200,000)
Fiscal Year 1995: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1994: ¥5,000,000 (Direct Cost: ¥5,000,000)
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| Keywords | Self-incompatibility / Brassica / SLG / SRK / Antisense / Kinase / Transformation / アンチセンス / 形質転換 / アンチセンス遺伝子 / アブラナ科植物 / S遺伝子 |
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| Research Abstract |
To calrify the molecular mechanism of self-incompatibility system of Brassica, this project aimed the analysis of the structures and functions of genes presumed to be associated with the S-locus.
1.Analysis of genes associated with self-incompatibility of Brassica.
From the cDNA libraries of stigma of B.campestris S8 and S12 strains, clones encoding SLG (S-locus glycorotein) and SRK (S-receptor kinase) were isolated and their siquences were established. Furthermore, the genomic DNA of SLG12, SLG9 and SRK9 were also cloned ANd their sequences were analyzed.
2.Transformation of the antisense gene of SLG.
A antisense constract for SLG8 was transformed to a strain of B.rapa with Agrobacterium-mediated system. In a transoformant obtained, the self-incompatibility was broken down with the action of the antisense gene. The gene was actively inherited to hte next generation through the crossing.
3.Expression of the kinase domain of SRK.
The inner cellular domain of SRK,kinase domain, was expresses as a fusion protein with GST.The expressed protein rvealted the activity of auto-phosphorylation in an in-vitro system.
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