Serrano L, Montejo de Garcini E, Hernández M A, Avila J
Eur J Biochem. 1985 Dec 16;153(3):595-600. doi: 10.1111/j.1432-1033.1985.tb09342.x.
Limited proteolysis of tubulin with subtilisin resulted in the removal of the carboxyl-terminal moiety of tubulin subunits. The remaining peptides from both alpha and beta tubulin lacking the carboxyl terminal did not bind to tau factor nor to MAP2 or MAP1. The carboxyl-terminal fragments bind to tau factor and MAP2 and both compete for the same binding sites in the tubulin molecule. Our results suggest that the carboxyl-terminal region of tubulin is a regulatory domain for the assembly of tubulin and the site for interaction with MAPs.
用枯草杆菌蛋白酶对微管蛋白进行有限的蛋白水解，导致微管蛋白亚基的羧基末端部分被去除。来自α和β微管蛋白且缺乏羧基末端的剩余肽段既不与tau因子结合，也不与MAP2或MAP1结合。羧基末端片段与tau因子和MAP2结合，并且两者在微管蛋白分子中竞争相同的结合位点。我们的结果表明，微管蛋白的羧基末端区域是微管蛋白组装的调节结构域以及与微管相关蛋白相互作用的位点。
