14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase
14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase
复制标题
DOI：
10.1006/bbrc.1996.5933
复制
发表时间：
1997-01-13
影响因子：
3.1
通讯作者：
Yasuda, H
中科院分区：
文献类型：
--
作者：
Honda, R;Ohba, Y;Yasuda, H
为了鉴定与小鼠weel激酶结合的蛋白质，将酵母“双杂交”系统与小鼠cDNA文库一起使用。利用weel激酶的羧基半，分离14-3-3 zeta蛋白。重组14-3-3 zeta在体外被证明与weel激酶结合。被cdc 2激酶磷酸化的weel激酶也与14-3-3 zeta蛋白结合。当weel激酶和14-3-3 zeta都转染到COS-1细胞中时，它们在细胞中形成复合物。通过表达来自weel激酶的不同长度的肽的双杂交系统测试结合所必需的weel激酶的序列。整个激酶结构域和羧基末端的序列被认为是结合所必需的。14-3-3 zeta蛋白在通过weel激酶调控G2期向M期转变中的作用尚待进一步阐明。(C)1997学术出版社
To identify proteins which bind to mouse weel kinase, the yeast ''two-hybrid'' system was used with a mouse cDNA library. Using the carboxyl half of weel kinase, the 14-3-3 zeta protein was isolated. Recombinant 14-3-3 zeta was demonstrated to bind to weel kinase in vitro. The weel kinase phosphorylated by cdc2 kinase also bound to 14-3-3 zeta protein. When both weel kinase and 14-3-3 zeta were transfected into COS-1 cells, they formed a complex in a cell. The sequence of weel kinase necessary for the binding was tested by a two hybrid system expressing different lengths of peptides derived from weel kinase. Both the entire kinase domain and a sequence in the carboxyl terminus was thought to be necessary for the binding. The function of 14-3-3 zeta protein remained to be elucidated in relation to the regulation of G2 to M phase transition through weel kinase. (C) 1997 Academic Press