Modification of Tryptophan Residues of Plant Class III Chitinases Involved in Enzyme Activity

DOI HANDLE オープンアクセス
  • 石黒 正恒
    九州大学農学部蛋白質化学工学
  • 山上 健
    九州大学農学部蛋白質化学工学
  • Tanigawa Miho
    Laboratory of Protein Chemistry and Engineering, Department of Genetic Resources Technology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
  • Tsutsumi Kazuki
    Laboratory of Protein Chemistry and Engineering, Department of Genetic Resources Technology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
  • 船津 軍喜
    九州大学農学部蛋白質化学工学
  • 大沼 貴之
    九州大学大学院生物資源環境科学府蛋白質化学工学
  • 麻生 陽一
    九州大学農学部蛋白質化学工学

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抄録

amino acids with a calculated molecular mass of 67kDa. The deduced amino acid sequence of T. halophila DnaK showed high similarities with the corresponding DnaK homologues of Lactococcus lactis, Lactobacillus sakei and Bacillus subtilis. Using a pET expression system, the T. halophila DnaK was overexpressed in Escherichia coli and the purified T.halophila DnaK was found to have ATPase activity. Northern hybridization analysis revealed that the transcription of dnaK gene was induceed by heat shock, and several transcripts were detected including a maximum size of tetra-cistronic mRNA 4.9-kb which represents the transcript complete dnaK operon. The amount of dnaK transcripts was also increased about 3.5-fold by high NaCl condition （3-4 M）, but not by the same concentration of KCI. These results suggest that the cloned DnaK surely acts as the functional molecular chaperone and play an important role in the salinity adaptation.

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詳細情報 詳細情報について

  • CRID
    1390853649614055552
  • NII論文ID
    110000018063
  • NII書誌ID
    AA00247166
  • DOI
    10.5109/24436
  • HANDLE
    2324/24436
  • ISSN
    00236152
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • IRDB
    • Crossref
    • CiNii Articles

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