2001 Fiscal Year Final Research Report Summary
Researches on ribozymes at molecular and atomic level
| Project/Area Number |
09278103
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas (A)
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| Allocation Type | Single-year Grants |
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| Research Institution | Kyoto University |
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Principal Investigator |
INOUE Tan Kyoto University, Graduate School of Biostudies, Professor, 大学院・生命科学研究科, 教授 (40114855)
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| Co-Investigator(Kenkyū-buntansha) |
SHIRAISHI Hideaki Kyoto University, Graduate School of Biostudies, Associate Professor, 大学院・生命科学研究科, 助教授 (90202118)
TANI Tokio Kyushu University, Graduate School of Science, Associate Professor, 大学院・理学研究科, 助教授 (80197516)
TAIRA Kazunari The University of Tokyo, Graduate School of Engineering, Professor, 大学院・工学系研究科, 教授 (10261778)
SAKAMOTO Kensaku The University of Tokyo, Graduate School of Science, Research Associate, 大学院・理学系研究科, 助手 (50240685)
SUZUKI Tsutomu The University of Tokyo, Graduate School of Frontier Sciences, Lecturer, 大学院・新領域創成科学研究科, 講師 (20292782)
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| Project Period (FY) |
1997 – 2000
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| Keywords | RNA / ribozyme / catakytic RNA / snRNA / RNP / group I introns / hammerhead ribozyme / splicing |
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| Research Abstract |
The molecular design, structure and reaction mechanism of the naturally occurring ribozymes were investigated. The minimal catalytic unit of Group I intron ribozymes was identified. The RNA folding pathways and the intermolecular long-range interactions of the intron were identified. In vitro selection te4chnique was successfully employed for producing artificial ribozymes and RNPs. Hammerhead ribozyme was engineered successfully for in vivo use. New gene discovery system was developed. Ribosomal RNAs of mammalian mitochondria and the corresponding protein components were identified and analyzed. It was elucidated that the binding of stalk proteins to rRNA in the ribosomal GTPase center is involved in formation of the functional structure of two RNA domains. These complexes affected not only elongation factor-binding site in the rRNA but also the functional structure of the decoding site. A gene coding for the Prp12 which interacts with Prp1 (pre-mRNA processing 1) of fission yeast which is a component of U4/U6 snRNP was cloned. As a result, it was elucidated that the interaction of U4/U6 snRNP with U2 snRNP which is necessary for conversion of a commitment complex to a spliceosome at the early stage of splicing depends on not only interaction due to hydrogen bonding between U2 and U6 snRNAs, but also interaction among proteins bound to the snRNAs.
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