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Domain structure, expressional regulation and autoimmunity of HSP90

Research Project

Project/Area Number 10671746
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Functional basic dentistry
Research InstitutionNagasaki University (1999)
Iwate Medical University (1998)

Principal Investigator

NEMOTO Takayuki  Nagasaki University, School of Dentistry, Professor, 歯学部, 教授 (90164665)

Co-Investigator(Kenkyū-buntansha) BABA Tomomi  Nagasaki University, School nof Dentistry, Instructor, 歯学部, 助手 (60189727)
ONO Toshio  Nagasaki University, School nof Dentistry, Instructor, 歯学部, 助手 (80050607)
永井 雅純  岩手医科大学, 歯学部, 助手 (00217960)
Project Period (FY) 1998 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 1999: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1998: ¥2,300,000 (Direct Cost: ¥2,300,000)
Keywordsstress protein / molecular chaperone / HSP90 / domain / systemic lupus erythematosus (SLE) / oligomer / dimer / 自己抗体 / ドメイン構造 / 骨芽細胞 / アイメフォーム
Research Abstract

By use of isoform-specific monoclonal antibodies, the expression of the two HSP90 isoforms was investigated on various rat tissues and osteoclasts and osteoblasts that were induced in alveolar bones of the experimental movement of rat molar teeth. As a result, the predominant and constitutive distribution of HSP90β and stress-induced expression of HSP90α in most murine tissues were demonstrated. We also investigated the domain structure of HtpG, an Esherichia coli homologue of mammalian HSP90 and its domain-domain interactions. HtpG had three major cleavage sites, Arg7-Gly8, Arg336-Glu337 and Lys552-Leu553, susceptible to trypsin. Thus, HtpG consists of three domains: Domain A, Metl-Arg336; Domain B, Glu337-Lys 552; Domain C, Leu553-Ser624. Three kinds of interactions work between the domains of a HtpG dimer: Domain B interacted both with Domain A and Domain C, and moreover, Domain B had a homodimeric interaction. The interaction between Domain B and Domain C was responsible for the dimer conformation of HtpG. Furthermore, Domain B was functionally and structurally divided into two parts: the N-terminal two-third (Glu337-Phe480) that interacted with Domain A and the C-terminal one-third (G1n481-Lys552) that interacted with Domain C. This study first demonstrated the domain structure of HtpG and the interactions between the domains. These characteristics seem to be common among HSP90-family member proteins.

Report

(3 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • Research Products

    (6 results)

All Other

All Publications (6 results)

  • [Publications] Maruya M.: "monomer arrangement in HSP90 dimer as determined by decoration with N- and C-terminal specific antibodies"Journal of Molecular Biology. 285. 903-097 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Maruya M: "Monomer arrangement in HSP90 dimer as determined by decoration with N- and C-terminal specific antbodies"Journal of Molecular Biology. 285. 903-907 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Maruya M.: "Monomer arrangement in HSP90 dimer as determined by decoration with N- and C-terminal specific antibodies"Journal of Molecular Biology. 285. 903-907 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] Maruya,M.et al.: "Monomer arrangement in HSP90 dimer as determined by decoration with N- and C-terminal specific antibodies." J.Mol.Biol.in press.

    • Related Report
      1998 Annual Research Report
  • [Publications] Nemoto,T.and Sato,N.: "Analysis of subunit structures of proteins by polyacrylamide gel electrophoresis." Anal.Biochem.265. 190-192 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Nemoto,T.and Sato,N.: "Oligomeric forms of the 90-kDa heat shock protein." Biochem.J.330. 989-995 (1998)

    • Related Report
      1998 Annual Research Report

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Published: 1998-04-01   Modified: 2016-04-21  

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