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Analysis of cellular function of HBP23 on redox regulation

Research Project

Project/Area Number 12670124
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field General medical chemistry
Research InstitutionNippon Medical School

Principal Investigator

ABE Yasuko  Nippon Medical School, Dept. Biochem. Mol. Biol., Lecturer, 医学部, 講師 (60089612)

Co-Investigator(Kenkyū-buntansha) MATSUMURA Tomihiro  Nippon Medical School, Dept. Biochem. Mol. Biol., Asisstant, 医学部, 助手 (20297930)
Project Period (FY) 2000 – 2001
Project Status Completed (Fiscal Year 2001)
Budget Amount *help
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2000: ¥2,000,000 (Direct Cost: ¥2,000,000)
Keywordsrat / HBP23 / peroxiredoxin / Peroxidase
Research Abstract

HBP23 (Heme Binding Protein, M.W. : 23kDa), a rat cytosolic protein with high binding affinity for heme, is a member of the peroxiredoxin family, which exhibits thioredoxin-dependent peroxidase activity. The mutants, Cys52Ser, Cys173Ser and Cys52-173Ser, did not show the activity, which was different from that of the mutant (Cys83Ser). A 2.6A-resolutin crystal structure of HBP23 (Cys83Ser) in oxidative form revealed a unique dimer structure in which Cys-52 forms a disulfide bond with Cys-173 from another subunit by C-terminal tail swapping. The internal disulfide bond was surrounding by the two arginine residues, Arg-123 and Arg-151. The mutations at the positions showed reduced activity. Thus, the cysteine residues are involved in the peroxidation catalysis and form a disulfide bond as an intermediate. The residues, Arg-123 and Arg-151 may display enhanced reactivity by interacting with Cys-52 due to decrease the level of pK. HBP23 interacts with heme in a 1 : 1 molar ratio of heme/protein. Thioredoxn-dependent peroxidase activity on HBP23 was inhibited in partially by heme. It was suggested that heme bound to the amino acid residue(s) of HBP23 by analysis of Resonance Raman spectra. Although the role of heme is not clear at the moment, it is of interest, because this protein is also induced by heme. The Western-blot analysis showed that HBP23 is a mixture of dimer and decamer in the rat liver cytosolic fraction.

Report

(3 results)
  • 2001 Annual Research Report   Final Research Report Summary
  • 2000 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] 広津晶子 他: "ペルオキシレドキシンの分子機能の構造的基盤"蛋白質核酸酵素. 45. 2463-2474 (2000)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2001 Final Research Report Summary
  • [Publications] S. Hirotsu, Y. Abe, T. Nishino, T. Hakoshima: "Structural basis of peroxiredoxin function"Protein, Nucleic acid & Enzyme. 45. 2463-2467 (2000)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2001 Final Research Report Summary
  • [Publications] K. Ichida: "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II"Biochem. Biophys. Res. Commun.. 282(5). 1194-1200 (2001)

    • Related Report
      2001 Annual Research Report
  • [Publications] 広津晶子 他: "ペルオキシレドキシンの分子機構の構造的基盤"蛋白質 核酸 酵素. 45(15). 2463-2474 (2000)

    • Related Report
      2000 Annual Research Report

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Published: 2000-04-01   Modified: 2016-04-21  

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