Expression and Thermal Stability Analysis of Peat1 and the 3 Deletion Mutants  

Peat1蛋白及其3个缺失突变体的表达与热稳定性分析（英文）

作　　者：李明勇[1] 邱德文[1] 曾洪梅[1] 杨秀芬[1] 

机构地区：[1]中国农业科学院植物保护研究所

出　　处：《Agricultural Science & Technology》2008年第1期32-34,38,共4页农业科学与技术（英文版）

基　　金：Supported by the“973”Program(2003CB114204);the Science and Technology Plan(D0706005040431)~~

摘　　要：[Objective] The research aimed to reveal the functions of NAC and UBA domains in Peatl＇s thermal stability. [Method] Fusion expression vectors of Pearl protein and the 3 deletion mutants were constructed. The recombinant plasmids were induced by IPTG and the target proteins （Peatl, Peatl-△CD99,Peatl-△ND49 and Pearl-△ND108 ）were expressed obtained by AKTA and its thermal stability was analyzed. [Result] The research found that 3 deletion mutants have good thermal stability like Pearl. [Conclusion] The research demonstrated that the coexistence of NAC or UBA domains is not necessary to thermal stability of Pearl protein , and they may give the protein particular stability structure seperately.从极细链格孢菌中提取出一种植物激活蛋白，后命名为Peatl，其分子量为35 kD。该蛋白具有良好的热稳定性。生物信息学分析显示，Peatl含有2个保守结构域，即NAC（Nascent polypeptide-associated complex）和UBA（Ubiquitin-associated）结构域。该文将Peatl在E.coli中进行克隆和表达，并构建3个缺失突变体，拟对赋予Peatl热稳定性的区域进行初步定位。

关 键 词：Peatl Deletion mutant Thermal stability 

分 类 号：Q51[生物学—生物化学]