Functional Analysis of the Chitin-binding Domain of a Family 19 Chitinase from<i>Streptomyces griseus</i>HUT6037: Substrate-binding Affinity and<i>cis</i>-Dominant Increase of Antifungal Function

  • ITOH Yoshikane
    <i>Department of Biosystem Science, Graduate School of Science and Technology, Niigata University</i>
  • KAWASE Tomokazu
    <i>Department of Biosystem Science, Graduate School of Science and Technology, Niigata University</i>
  • NIKAIDOU Naoki
    <i>Department of Biosystem Science, Graduate School of Science and Technology, Niigata University</i>
  • FUKADA Harumi
    <i>Laboratory of Biophysical Chemistry, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University</i>
  • MITSUTOMI Masaru
    <i>Department of Applied Biological Sciences, Faculty of Agriculture, Saga University</i>
  • WATANABE Takeshi
    <i>Department of Biosystem Science, Graduate School of Science and Technology, Niigata University</i>
  • ITOH Yoshifumi
    <i>Division of Applied Microbiology, National Food Research Institute</i>

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  • Functional Analysis of the Chitin-binding Domain of a Family 19 Chitinase from Streptomyces griseus HUT6037: Substrate-binding Affinity and cis-Dominant Increase of Antifungal Function.

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  Chitinase C (ChiC) is the first bacterial family 19 chitinase discovered in Streptomyces griseus HUT6037. While it shares significant similarity with the plant family 19 chitinases in the catalytic domain, its N-terminal chitin-binding domain (ChBDChiC) differs from those of the plant enzymes. ChBDChiC and the catalytic domain (CatDChiC), as well as intact ChiC, were separately produced in E. coli and purified to homogeneity. Binding experiments and isothermal titration calorimetry assays demonstrated that ChBDChiC binds to insoluble chitin, soluble chitin, cellulose, and N-acetylchitohexaose (roughly in that order). A deletion of ChBDChiC resulted in moderate (about 50%) reduction of the hydrolyzing activity toward insoluble chitin substrates, but most (about 90%) of the antifungal activity against Trichoderma reesei was abolished by this deletion. Thus, this domain appears to contribute more importantly to antifungal properties than to catalytic activities. ChBDChiC itself did not have antifungal activity or a synergistic effect on the antifungal activity of CatDChiC in trans.<br>

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