石kariensis (01B)雪霉菌抗冻蛋白异构体的诱变研究。蛋白质:结构与功能,海报,第52届日本生物物理学会年会(BSJ2014)

Jing Cheng, Yuichi Hanada, H. Kondo, S. Tsuda
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引用次数: 0

摘要

抗冻蛋白(AFPs)通过抑制冰晶生长,促进冰冻环境下生物的低温生存。在这项研究中,我们重点研究了一种真菌AFP,称为TisAFP,它是从一种嗜冷的雪霉菌,Typhula ishikariensis中分泌的。报道了7种具有高序列同一性的TisAFP亚型。值得注意的是,基于荧光的冰平面亲和力(FIPA)分析显示,TisAFP8的冰结合特异性与其他蛋白有很大不同。为了弄清是什么决定了TisAFP8的独特性,我们对TisAFP8进行了诱变实验,特别是对构建其推测的冰结合位点的残基进行了诱变实验。这些数据表明TisAFP8向内指向残基的重要性,而不仅仅是向外指向残基。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
3P043 Mutagenesis study of an antifreeze protein isoform from a snow-mold fungus, Typhula ishikariensis(01B. Protein: Structure & Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))
Antifreeze proteins (AFPs) facilitate cold-survival of the organisms living under freezing environment by inhibiting ice crystal growth. In this study, we focused on a fungal AFP denoted TisAFP secreted from a psychrophilic snow-mold fungus, Typhula ishikariensis. It reported seven isoforms of TisAFP that share a high sequence identity. Significantly, fluorescencebased ice plane affinity (FIPA) analysis showed that the ice binding specificity of TisAFP8 is quite different from the others. To clarify what determines the uniqueness of TisAFP8, we performed mutagenesis experiments on TisAFP8, especially on the residues constructing its putative ice-binding site. The data suggested an importance of inward pointing residues not just outward pointing residues of TisAFP8.
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