| Project/Area Number |
17580006
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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 | Yokohama City University (2006-2007)
Nara Institute of Science and Technology (2005) |
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Principal Investigator |
ISSHIKI Masayuki Yokohama City University, 木原生物学研究所, Associate professor (10314543)
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| Co-Investigator(Kenkyū-buntansha) |
SHIMAMOTO Ko Nara Institute of Science and Technology, バイオサイエンス研究科, Professor (10263427)
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| Project Period (FY) |
2005 – 2006
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2006: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2005: ¥1,800,000 (Direct Cost: ¥1,800,000)
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| Keywords | Waxy / Amylose / Splicing / Rice / dull / Cap-binding protein / Spliceosome / FCA / PRP1 / CBP20 / GFP / Yeast-two hybrid / 遺伝子単離 / RNAi |
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| Research Abstract |
Du1 gene encodes a homolog of the human U5 samll ribonucleoprotein-associated 102kD (U5-102kD) protein and yeast Prp1p that is an essential pre-mRNA splicing factor for spliceosome assembly. Moreover, Du3 gene was identified that it encodes the rice homolog of a cap-binding protein 20kD subunit (CBP20) that is a component of the heterodimeric nuclear cap-binding complex (CBC) playing role in pre-mRNA splicing, RNA nucler export, and nonsense-mediated decay (NMD).
1. Yeast two-hybrid experiment showed that Dul protein can interact with a rice PRP31 homolog. This result suggests that DU1-OsPRP31 complex may play an important role for assembly of U4/U6-U5 tri-snRNP in plant the same as human.
2. Du3 mutation and RNAi affected the expression pattern of three alternative transcripts of OsFCA, which is encoded an RNA binding protein. The results of RT-PCR analysis suggested that Du3 may control 3' end processing and polyadenylation at intron 3
3. Dul and Du3 proteins localized in nuclear speckles.
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