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Structural study of the peroxisomal membrane protein specific transport sysmem in the peroxisome biogenesis

Research Project

Project/Area Number 25440030
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Structural biochemistry
Research InstitutionKyoto Sangyo University (2015)
Kyushu University (2013-2014)

Principal Investigator

NIWA Hajime  京都産業大学, 総合生命科学部, 研究員 (30610266)

Co-Investigator(Kenkyū-buntansha) FUJIKI Yukio  九州大学, 生命防御医学研究所, 特任教授 (70261237)
Project Period (FY) 2013-04-01 – 2016-03-31
Project Status Completed (Fiscal Year 2015)
Budget Amount *help
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2015: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Keywordsタンパク質複合体 / 結晶構造解析 / 高速AFM / ペルオキシソーム / ミトコンドリア / AAAタンパク質 / 立体構造解析 / 蛋白質複合体 / 蛋白質相互作用 / 蛋白質 / 高速原子間力顕微鏡
Outline of Final Research Achievements

To analysis the quality control of mitochondria outer-membrane, we have crystallized Yeast Msp1 and human homologue ATAD1. Yeast Msp1 can be almost solved the structure and revealed the atomic-model which is similar to the p97-D2 domain. Pex7p is the cytosolic receptor protein that is essential for the import of peroxisomal proteins. Newly isolated as a binding protein of Pex7p, termed P7BP2, was found to be a disk-like ring with a central hole under high-speed atomic force microscope (AFM), and implicate that P7BP2 is a novel dynein-type AAA+, whose domains are arranged into a pseudo-hexameric ring structure.

Report

(4 results)
  • 2015 Annual Research Report   Final Research Report ( PDF )
  • 2014 Research-status Report
  • 2013 Research-status Report
  • Research Products

    (5 results)

All 2015 2014 Other

All Journal Article (3 results) (of which Peer Reviewed: 3 results,  Open Access: 2 results,  Acknowledgement Compliant: 2 results) Presentation (2 results)

  • [Journal Article] Pex11p mediates peroxisomal proliferation by promoting deformation of the lipid membrane2015

    • Author(s)
      Yoshida Y., Niwa H., Honsho M., Itoyama A., Fujiki Y.
    • Journal Title

      Biol. Open

      Volume: in press

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Open Access / Acknowledgement Compliant
  • [Journal Article] Mild reduction of plasmalogens causes rhizomelic chondrodysplasia punctata: Functional characterization of a novel mutation2014

    • Author(s)
      Noguchi, M., Honsho, M., Abe, Y., Toyama, R., Niwa, H., Sato, Y., Ghaedi, K., Rahmanifar, A., Shafeghati, Y., and *Fujiki, Y.
    • Journal Title

      Journal of Human Genetics

      Volume: 59 Issue: 7 Pages: 387-392

    • DOI

      10.1038/jhg.2014.39

    • Related Report
      2014 Research-status Report
    • Peer Reviewed / Open Access / Acknowledgement Compliant
  • [Journal Article] Inter-ring rotations of AAA ATPase p97 revealed by electron cryomicroscopy2014

    • Author(s)
      Heidi O. Yeung, Andreas Forster, Cecilia Bebeacua, Hajime Niwa, Caroline Ewens, Ciaran McKeown, Xiaodong Zhang and Paul S. Freemont
    • Journal Title

      Open Biol

      Volume: 4 Issue: 3 Pages: 130142-130142

    • DOI

      10.1098/rsob.130142

    • Related Report
      2013 Research-status Report
    • Peer Reviewed
  • [Presentation] A novel AAA ATPase interacting with Pex7 modulates plasmalogen synthesis

    • Author(s)
      Hajime Niwa, Yasuhiro Miyauchi-Nanri, Masanori Hosho, and Yukio Fujiki
    • Organizer
      10th International Conference on AAA+ Protein From Mecahnisms and Disease to Targets
    • Place of Presentation
      Comundo Conference Centre, Neuss, Germany
    • Related Report
      2013 Research-status Report
  • [Presentation] Structural study of peroxisomal membrane protein import

    • Author(s)
      Hajime Niwa
    • Organizer
      IMEG seminars & Minisymposium: Recent and future advances in high-speed AFM imaging of ATP/GTP-driven molecular machinery
    • Place of Presentation
      Institute of Molecular Embryology and Genetics, Kumamoto University
    • Related Report
      2013 Research-status Report

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Published: 2014-07-25   Modified: 2019-07-29  

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