Functional Analysis of Two Processed Fragments of Bacillus thuringiensis Cry11A Toxin

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The 70-kDa protoxin of Cry11A, a dipteran-specific insecticidal protein, was processed by trypsin into 36- and 32-kDa fragments. To investigate the potent function of the two processed fragments, a GST (Glutathione-<I>S</I>-transferase) fusion protein of each polypeptide was constructed. While neither the 36- nor the 32-kDa fragment was toxic to <I>Culex pipiens</I> larvae, coexpression of the two fragments restored the insecticidal activity. Furthermore, the coprecipitation experiment demonstrated that the 36-kDa fragment was associated with the 32-kDa fragment. It was, therefore, shown that the coexistence of the two processed fragments of Cry11A was essential for the toxicity. The mutant of the 36-kDa fragment lacking the region from Gly<SUP>257</SUP> to Arg<SUP>360</SUP> bound to the 32-kDa fragment but the coexpression with the 32-kDa fragment resulted in no toxicity, suggesting that this region was involved in insecticidal activity.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 68(3), 523-528, 2004-03-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10013142578
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    6904117
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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