1. Hydroxyl groups of threonines contribute to the activity of Ca^<2+>-depdendent type II antifreeze protein

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  • YASUI Masanori
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST):Division of Biological Sciences, Graduate School of Science, Hokkaido University
  • TAKAMICHI Manabu
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST):Division of Biological Sciences, Graduate School of Science, Hokkaido University
  • MIURA Ai
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST)
  • NISHIMIYA Yoshiyuki
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST)
  • KONDO Hidemasa
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST)
  • TSUDA Sakae
    Functional Protein Research Group, Research Institute of Genome-based Biofactory, National Institute of Advanced Industrial Science and Technology (AIST):Division of Biological Sciences, Graduate School of Science, Hokkaido University

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  • Hydroxyl groups of threonines contribute to the activity of Ca[2+]-depdendent type 2 antifreeze protein

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Type II antifreeze protein from herring and smelt (AFPII) exhibits thermal hysteresis (TH) activity when the protein is saturated with Ca^<2+>. The ice-binding site of AFPII consists of Thr96, Thr98, and two Ca^<2+>-coordinating residues. Here we examined TH activity of AFPII from Japanese smelt (Hypomesus nipponensis) and its mutant proteins, T96S, T96V, T96A, T98S, T98V, and T98A. Note that T96S denotes a mutant whose Thr96 is replaced with Ser. It appeared that substitution of Thr96 with Ser and Val retained 90% and 45% of TH activity, respectively, while it becomes inactive when substituted with Ala. For Thr98, Ser substitution had no significant influence on TH, whereas it becomes less than 20% by Val and Ala substitutions. These results suggest that hydroxyl group rather than methyl group of Thrs are essential for TH activity of AFPII, which is quite distinct from the other types of AFP.

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