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Structural Study on the early stage spliceosomal complex

Research Project

Project/Area Number 14580620
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Structural biochemistry
Research InstitutionRIKEN (The Institute of Physical and Chemical Research)

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)

Project Period (FY) 2002 – 2003
Project Status Completed (Fiscal Year 2003)
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)
KeywordsU2AF / 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
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.

Report

(3 results)
  • 2003 Annual Research Report   Final Research Report Summary
  • 2002 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Yutaka Muto, Daniel Krummel, Chris Oubridge, David Neuhaus, Kiyoshi Nagai: "The structure and biochemical properties of the human spliceosomal protein U1C"J.Mol.Biology. In press. (2004)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Yutaka Muto, Daniel Krummel, Chris Oubridge, David Neuhaud, Kiyoshi Nagai: "The structure and biochemical properties of the human spliceosomal protein U1C"J.Mol. Biology. (In press). (2004)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2003 Final Research Report Summary
  • [Publications] Yutaka Muto^<1, 2, 7>, Daniel Krummel^<17>Chris Oubridge^1, David Neuhaus^1, Kiyoshi Nagai: "The structure and biochemical properties of the human spliceosomal protein U1C"J.Mol.Biology. In press. (2004)

    • Related Report
      2003 Annual Research Report
  • [Publications] Aya Kitamura et al.: "Solution Structure of an RNA fragment with the P7/P9.0 region and the 3'-terminal guanosine of the Tetrahymena group I intron"RNA. 8. 440-451 (2002)

    • Related Report
      2002 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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