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Functional analysis of rice proteins which bind to the α subunit of nuclear transport complex.

Research Project

Project/Area Number 11640645
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 植物生理
Research InstitutionNIIGATA UNIVERSITY

Principal Investigator

IWASAKI Toshisuke  Niigata University, Faculty of Science, Associate Professor, 理学部, 助教授 (00201947)

Project Period (FY) 1999 – 2000
Project Status Completed (Fiscal Year 2000)
Budget Amount *help
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2000: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1999: ¥2,100,000 (Direct Cost: ¥2,100,000)
KeywordsNuclear protein / Importin α-binding protein / Light-responsive gene expression / Protein-protein interaction / Rice / Affinity chromatography / TPR sequence / Nuclear localization signal / インボーティンα結合タンパク質 / タンパク質核輸送 / インポーティンα
Research Abstract

The purpose of this research is to identify a novel nuclear protein which might be involved in the light-response in rice plants, by isolating proteins that bind to rice importin α 1a (IMP α 1a) whose expression is down-regulated by light. Below are the results.
1. Analysis of an IMP α 1a-binding protein, IABP4, which has been isolated by cDNA screening by Far western method.
(1) Determination of the full cDNA sequence : The IABP4 cDNA contained the entire coding sequence for a novel protein of predicted molecular mass of 122 kDa, and the homologous gene was found on the chromosome 2 of Arabidopsis thaliana.. In the N-terminal region containing TPR motifs, IABP4 protein shows high homology to a mouse nuclear phosphoprotein, TSP, whereas the similarity is low in the C-terminal region which contains the SH2-binding domain in mouse TSP, suggesting that the IABP4 protein is not necessarily homologous in function to TSP.The C-terminal part contains a putative nuclear localization signal.
(2) Analysis of gene expression : The result of RT-PCR indicated that the IABP4 transcript level decreases by illuminating dark-grown seedlings of rice.
(3) Analysis of binding to IMP α 1a : Usins purified recombinant proteins expressed in E.coil, the binding assay with native polyacrylamide gel electrophoresis demonstrated the complex formation between the C-terminal part of IABP4 and GST-IMP α 1a.
Further experiments are required for determination of nuclear localization and the in planta function of the IABP4 protein.
2. By another approach using affinity chromatography, several IMP α 1a-binding proteins were isolated from etiolated rice seedlings and the N-terminal sequences of three of them were determined. For one protein with homology to proline-rich protein, the corresponding cDNA was isolated and its expression was found to be down-regulated by light in dark-grown seedlings.

Report

(3 results)
  • 2000 Annual Research Report   Final Research Report Summary
  • 1999 Annual Research Report
  • Research Products

    (3 results)

All Other

All Publications (3 results)

  • [Publications] Jiang,C.J.: "Molecular cloning of a novel importin α homologue from rice, by which COP1 NLS-protein is preferentially nuclear imported."Journal of Biological Chemistry. (印刷中). (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Jiang, C.J., Shoji, K., Matsuki, R., Baba, A., Inagaki, N., Ban, H., Iwasaki, T., Imamoto, N., Yoneda, Y., Deng, X.W., and Yamaoto, N.: "Molecular cloning of a novel importin α from rice, by which COP1 NLS-protein is preferentially nuclear imported."Journal of Biological Chemistry. (in press). (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2000 Final Research Report Summary
  • [Publications] Jiang,C.J.: "Molecular cloning of a novel importin α homologue from rice, by which COP1 NLS-protein is preferentially nuclear imported."Journal of Biological Chemistry. (印刷中). (2001)

    • Related Report
      2000 Annual Research Report

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Published: 1999-04-01   Modified: 2016-04-21  

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