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2006 Fiscal Year Final Research Report Summary

Protein conformational changes and molecular chaperone

Research Project

Project/Area Number 14037241
Research Category

Grant-in-Aid for Scientific Research on Priority Areas

Allocation TypeSingle-year Grants
Review Section Biological Sciences
Research InstitutionTottori University

Principal Investigator

KAWATA Yasushi  Tottori University, Faculty of Engineering, Professor (40177697)

Co-Investigator(Kenkyū-buntansha) MIZOBATA Tomohiro  Tottori University, Faculty of Engineering, Associate Professor (50263489)
HONGO Kunihiro  Tottori University, Faculty of Engineering, Assistant Professor (80335504)
Project Period (FY) 2002 – 2006
KeywordsMolecular chaperone / Chaperonin / Conformational change / Amyloid fibril / Folding / Oligomeric protein / Thermostable enzyme / Ncurodegenerative disease
Research Abstract

In order to understand how protein tertiary structure that is responsible for biofunction occurs and how molecular chaperones are involved in the event, we studied stabilities and conformational changes of various proteins, and clarified molecular mechanism of protein amyloid fibril formation. Furthermore, we studied functional mechanism of molecular chaperone, especially, chaperonins in detail, and obtained following results.
1. Study on chaperonin mechanism: We have studied in detail structure and function relationship of group I chaperonin GroEL from E. coli and group II chaperonins from hyper-thermostable strains, from protein science and biophysical points of view. We have found that domain movements of GroEL are very important for the function and that cobalt and manganese ions are novel factors for nucleotide hydrolysis activity and substrate refolding function of group II chaperonin.
2. Study on mechanism of protein amyloid fibril formation: We have found that oligomeric protein … More GroES, that is a non-related protein to disease, formed typical amyloid fibrils under unfolded conditions, and elucidated the fibril formation mechanism in terms of molecular compactness. Furthermore, we studied fibril formation mechanism of α-synuclein, that is a causative protein of Parkinson's disease, and proved that the amyloid fibril formation of α-synuclein is accelerated markedly in the presence of preformed seeds of other different protein's fibrils.
3. Study on structure and stability of oligomeric protein: We have determined the X-ray crystal structure of thermostable aspartase enzyme, and elucidated the mechanism of thermostability and active site structure of the enzyme comprising from 4 identical subunits. On the other hand, we studied solution structure and molecular unfolding mechanism of E. coli co-chaperonin GroES heptamer at high protein concentrations by using small angle X-ray scattering. Furthermore, we clarified that the subunit interaction is quite important for the total structural stability. Less

  • Research Products

    (10 results)

All 2006 2005 2004 2003

All Journal Article (6 results) (of which Peer Reviewed: 3 results) Presentation (2 results) Book (2 results)

  • [Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins : Implications for the Mechanism of Transmissible Conformational Diseases2005

    • Author(s)
      Hisashi Yagi, et al.
    • Journal Title

      J. Biol. Chem. 280

      Pages: 38609-38616

    • Description
      「研究成果報告書概要(和文)」より
    • Peer Reviewed
  • [Journal Article] Amyloid Fibril Formation of α-Synuclein is Accelerated by Preformed Amyloid Seeds of Other Proteins: Implications for the Mechanism of Transmissible Conformational Diseases2005

    • Author(s)
      Hisashi Yagi, Eiko Kusaka, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
    • Journal Title

      Journal of Biological Chemistry 280(46)

      Pages: 38609-38616

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain : Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004

    • Author(s)
      Masaaki Taniguchi, et al.
    • Journal Title

      J. Biol. Chem. 279

      Pages: 16368-16376

    • Description
      「研究成果報告書概要(和文)」より
    • Peer Reviewed
  • [Journal Article] Stopped-Flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain: Relationships between Movements in the Apical Domain and the Quaternary Structure of GroEL2004

    • Author(s)
      Masaaki Taniguchi, Tatsunari Yoshimi, Kunihiro Hongo, Tomohiro Mizobata, Yasushi Kawata
    • Journal Title

      Journal of Biological Chemistry 279(16)

      Pages: 16368-16376

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Structural Stability and Solution Structure of Chaperonin GroES Heptamer Studied by Synchrotron Small-Angle χ-Ray Scattering2003

    • Author(s)
      Takashi Higurashi, et al.
    • Journal Title

      J. Mol. Biol. 333

      Pages: 605-620

    • Description
      「研究成果報告書概要(和文)」より
    • Peer Reviewed
  • [Journal Article] Structural Stability and Solution Structure of Chaperonin GroES Heptamer Studied by Synchrotron Small-Angle X-Ray Scattering2003

    • Author(s)
      Takashi Higurashi, Yuzuru Hiragi, Kaoru Ichimura, Yasutaka Seki, Kunitsugu Soda, Tomohiro Mizobata, Yasushi Kawata
    • Journal Title

      Journal of Molecular Biology 333(3)

      Pages: 605-620

    • Description
      「研究成果報告書概要(欧文)」より
  • [Presentation] Molecular mechanism of amyloid fibril formation2006

    • Author(s)
      Yasushi Kawata
    • Organizer
      Collegium Internationale Neuro-Psychopharmacologicum (CINP)Asia pacific Regional Meeting
    • Place of Presentation
      Pattaya, Thailand
    • Year and Date
      2006-03-16
    • Description
      「研究成果報告書概要(和文)」より
  • [Presentation] Molecular mechanism of amyloid fibril formation2006

    • Author(s)
      Yasushi Kawata.
    • Organizer
      Collegium Internationale Neuro-Psychopharmacologicum (CINP) Asia pacific Regional Meeting
    • Place of Presentation
      Pattaya, Thailand
    • Year and Date
      2006-03-16
    • Description
      「研究成果報告書概要(欧文)」より
  • [Book] タンパク質工学2004

    • Author(s)
      加藤昭夫, 他
    • Total Pages
      307
    • Publisher
      医学出版
    • Description
      「研究成果報告書概要(和文)」より
  • [Book] Protein Engineering2004

    • Author(s)
      Akio Kato, Shigeru Utsumi, Toshihiko Utsumi, Yasushi Kawata, Yuriko Yamagata, Akihiko Yamagishi, Masaaki Yoshikawa
    • Total Pages
      307
    • Publisher
      Igakushuppan Co.
    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2010-06-09  

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