Structural Study on the early stage spliceosomal complex
| Project/Area Number |
14580620
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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 |
Structural biochemistry
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| Research Institution | RIKEN (The Institute of Physical and Chemical Research) |
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Principal Investigator |
MUTO Yutaka RIKEN (The Institute of Physical and Chemical Research), Stable Isotopes Team, Team Leader, 標識技術高度化研究チーム・リームリーダー (30192769)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2003: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2002: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | U2AF / U2 snRNP / SAP155 / p14 / U1 snRNP / U1C / NMR / SF3a / SURPドメイン / SF4 / SF3a 120K / スプライシング / U2AF蛋白質 / U1snRNP / U1C蛋白質 / セルフスプライシング / グループIイントロン / Znフィンガー |
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| Research Abstract |
Eukaryotic post-transcriptional events, such as splicing, transport, and life time regulation of mRNAs, are important for regulation of gene expression and cell differentiation. The splicing of pre-mRNA is one of the important events, which remove the stretches of non-coding RNA before the RNA can be translated into protein. In the early stage in the splicing reaction, 5' splicing site have to be recognized by U1 snRNP,3' splicing site have to be recognized by U2AF protein and the branch site have to be recognized by U2 snRNP. On this study, we investigate the structure of protein which are involved in these components. 1.SURP domain is mainly observed in the splicing machinery (for example U2 snRNP). We determined the structure of SURP domain in SF4 protein. 2.We have tried to reconstitute the p14-SAP155 complex. By NMR method, we confirmed that the complex are successfully reconstituted. 3.In addition, for the structural study of U2AF protein, we could establish the protocol for the reconstitution of U2AF 4.U1C is the one component of the U1 snRNP. In order to gain the information about the interaction for U1-C protein, we have investigated the structure of the N-terminal (1-65) segment of the U1-C protein. And we determined the tertially structure of U1-C (1-61) proteins by homonuclear NMR methods.
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Report
(3 results)
Research Products
(4 results)
