拟南芥TAK蛋白激酶的结构预测与功能分析  

Structure Prediction and Function Analysis of TAK Kinase in Arabidopsis

作　　者：蒋佳宏[1] 王东[1] 胡源[1] 杜林方[1,2] 

机构地区：[1]四川大学生物资源与生态环境教育部重点实验室,成都610064 [2]四川大学纳米生物医学技术与膜生物学研究所,成都610041

出　　处：《应用与环境生物学报》2009年第5期610-614,共5页Chinese Journal of Applied and Environmental Biology

基　　金：教育部新世纪人才支持计划(No.NCET-04-0861);四川大学"985"项目资助~~

摘　　要：TAK1、TAK2和TAK3属于TAK蛋白激酶家族,由拟南芥核基因编码,其中TAK1参与了主要捕光色素复合物LHCⅡ蛋白磷酸化调控与光系统的状态转移.本文使用生物信息学手段对TAK1、TAK2和TAK3蛋白进行了较为系统的分析,发现TAK1、TAK2和TAK3为单次跨膜蛋白,具有保守的激酶活性域、疏水性强的N端跨越类囊体膜、亲水性高的C端处于基质中等特点.在PDB中找到了不少与TAK1、TAK2和TAK3同源性大于30%的蛋白序列,其中大部分也带有酪氨酸激酶保守域,使用同源建模的方法,建立了拟南芥蛋白激酶TAKs核心结构域的三维结构,围绕蛋白激酶的结构和作用机制关系进行了探讨,设计出多肽抗体,并进行蛋白印迹检测抗体的专一性,为TAKs蛋白激酶进一步的功能研究奠定了基础.TAK1, TAK2 and TAK3 belong to TAK kinase family and are nuclear-encoded kinases. TAK1 is involved in the phosphorylation of LHCII and the state transitions. Few studies on the structure or function of TAKs have been done because they are membrane combined proteins. In this research, TAKs were studied using a systematical bioinformatical method and all the members of TAK kinase family were found with a hydrophobic N-terminal connected with a transmembrane region located in thylakoid membrane and a hydrophilic C-terminal （kinase catalytic domains） on the stromal side of thylakoid. Lots of sequences which contained the same TyrKc kinase catalytic domains with a similarity more than 30% were found in PDB, and three dimensional structures of core domains of TAK1, TAK2 and TAK3 were then predicted by using homologous modeling method. The analysis of the relationship between the structure and function of TAKs provided the foundation for further studying the functions of TAK1, TAK2 and TAK3. We designed an antibody on the base of prediction of the three dimensional structures, and its western blotting showed that there was an immunoaffinity reaction. Fig 5, Tab 1, Ref 15

关 键 词：TAK 磷酸化 LHCII 核心结构域 同源建模 抗体 

分 类 号：Q946[生物学—植物学]