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Three-dimensional structure and Molecular Evolution of Tandem repeals within Ice Nucleation Proteins

Research Project

Project/Area Number 13680746
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Biophysics
Research InstitutionSapporo Medical University

Principal Investigator

MATSUSHIMA Norio  Sapporo Medical University, School of Health Sciences, Professor, 保健医療学部, 教授 (60137403)

Co-Investigator(Kenkyū-buntansha) NITTA Katsutoshi  Graduate School of Science, Hokkaido University, Professor, 大学院・理学研究科・生物科学専攻, 教授 (80001858)
Project Period (FY) 2001 – 2002
Project Status Completed (Fiscal Year 2002)
Budget Amount *help
¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 2002: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2001: ¥1,500,000 (Direct Cost: ¥1,500,000)
KeywordsIce nucleation protein / Tandem repeats / Loop structure / NMR / Glycine-rich proteins / Molecular evolution / 氷核タンパク質 / タンデムリピート / 核磁気共鳴法(NMR)
Research Abstract

Certain bacteria nucleate the crystallization of ice. The ice-nucleation activity is conferred by a protein (ice nucleation protein ; INP). The amino acid sequences of the INPs with molecular weights near 120kDa have a central repeating domain (comprising approximately 81% of the total sequence). The repeating domain consists of tandem repeats with the consensus sequence of AxxxSxxx. The structure of the INPs is still unknown. The purpose of the present study is to investigate the evolution and the structure of the INPs. First, we performed, comparative sequence analysis of ten INPs in details. The analysis revealed that the repeating domain is separated into four subdomains (R^c, R^1, R^2 and R^N). On the basis of this result, the evolutionary history was discussed. Secondly, we performed NMR experiments of synthetic peptide H-SGLRSVLTAGYGSSLISGRRSSLT-OH corresponding to sections of the R^N subdomain. The NMR results indicated the presence of a loop conformation in the sequence of LTAGY.

Report

(3 results)
  • 2002 Annual Research Report   Final Research Report Summary
  • 2001 Annual Research Report
  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] Kumaki Y, Matsushima N, Yoshida H, Nitta K, Hikichi K: "Structure of the YSPTSPS repeat containing two SPXX motifs in the CTD of RNA polymerase II. NMR studies of cyclic model peptides reveal that SPTS turn is more stable than SPSY in water"Biochim. Biophys. Acta.. 1548(1). 81-93 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Mitsuzawa H, Wada I, Sano H, Iwaki D, Murakami S, Himi T, Matsushima N, Kuroki Y: "Extracellular Toll-like receptor 2 region containing serine^<40>-isoleucine^<64> but not cysteine^<30>-serine^<39> is critical for the recognition of Staphylococcus aureus peptidoglycan"J. Biol. Chem.. 276(44). 41350-41356 (2001)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Hayashi N, Matsubara M, Jinbo Y, Titani K, Izumi Y, Matsushima N.: "Nef of HIV-1 interacts directly with calcium-bound calmodulin"Protein Sci.. 11(3). 529-537 (2002)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Hayashi N, Matsubara M, Jinbo Y, Titani K, Izumi Y, and Matsushima N: "Nef of HIV-1 interacts directly with calcium-bound calmodulin"Protein Sci.. 11(3). 529-537 (2002)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Kumaki Y, Matsushima N, Yoshida H, Nitta K, and Hikichi K: "Structure of the YSPTSPS repeat containing two SPXX motifs in the CTD of RNA polymerase II. NMR studies of cyclic model peptides reveal that SPTS turn is more stable than SPSY in water"Biochim.Biophys.Acta.. 1548(1). 81-93 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Mitsuzawa H, Wada I, Sano H, Iwaki D, Murakami S, Himi T, Matsushima N, and Kuroki Y.: "Extracellular Toll-like receptor 2 region containing serine^<40>-isoleucine^<64> but not cysteine^<30>-serine^<39> is critical for the recognition of Staphylococcus aureus peptidoglycan"J.Biol.Chem.. 276(44). 41350-42356 (2001)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2002 Final Research Report Summary
  • [Publications] Kumaki Y, Matsushima N, Yoshida H, Nitta K, Hikichi K.: "Structure of the YSPTSPS repeat containing two SPXX motifs in the CTD of RNA polymerase II. NMR studies of cyclic model peptides reveal that SPTS turn is more stable than SPSY in water"Biochim. Biophys. Acta.. 1548(1). 81-93 (2001)

    • Related Report
      2002 Annual Research Report
  • [Publications] Mitsuzawa H, Wada I, Sano H, Iwaki D, Murakami S, Himi T, Matsushima N, Kuroki Y: "Extracellular Toll-like receptor 2 region containing serine^<40>-isoleucine^<64> but not cysteine^<30>-serine^<39> is critical for the recognition of Staphylococcus aureus peptidoglycan"J. Biol. Chem.. 276(44). 41350-41356 (2001)

    • Related Report
      2002 Annual Research Report
  • [Publications] Hayashi N, Matsubara M, Jinbo Y, Titani K, Izumi Y, Matsushima N.: "Nef of HIV-1 interacts directly with calcium-bound calmodulin"Protein Sci.. 11(3). 529-537 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Hayashi N, Matsubara M, Jinbo Y, Titani K, Izumi Y, Matsushima N.: "Nef of HIV-1 interacts directly with calcium-bound calmodulin"Protein Sci. 11(3). 529-537 (2002)

    • Related Report
      2001 Annual Research Report
  • [Publications] Mitsuzawa H, Wada I, Sano H, Iwaki D, Murakami S, Himi T, Matsushima N, Kuroki Y.: "Extracellular Toll-like receptor 2 region containing serine^<40>-isoleucine^<64> but not cysteine^<30>-serine^<39> is critical for the recognition of Staphylococcus aureus peptidoglycan"J. Biol. Chem.. 276(44). 41350-41356 (2001)

    • Related Report
      2001 Annual Research Report
  • [Publications] Kumaki, Y., Matsushima, N., Yoshida, H., Nitta, K., Hikichi, K.: "Structure of the YSPTSPS repeat containing two SPXX motifs in the CTD of RNA polymerase II : NMR studies of cyclic model peptides reveal that SPTS turn is more stable than SPSY in water"Biochim. Biophys. Acta.. 1548(1). 81-93 (2001)

    • Related Report
      2001 Annual Research Report

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Published: 2001-04-01   Modified: 2016-04-21  

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