New axonemal dynein heavy chains from Tetrahymena thermophila.
New axonemal dynein heavy chains from Tetrahymena thermophila.
复制标题
来自嗜热四膜虫的新轴丝动力蛋白重链。
DOI：
10.1111/j.1550-7408.1999.tb04598.x
复制
发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Pennock,DG
中科院分区：
文献类型：
--
作者：
Mobberley,PS;Sullivan,JL;Angus,SP;Kong,X;Pennock,DG
从四膜虫的轴丝中提取出两种动力蛋白。22 S动力蛋白含有三条重链（HC），在蔗糖梯度中沉积在22 S处，并构成外臂。14 S动力蛋白含有2 - 6个HC，在14 S处沉积，被认为有助于内臂的形成。我们已经确定了两个大的蛋白质，从四膜虫轴索中提取高盐，并在大约18 S沉淀在一起。这两个大的蛋白质在ATP和钒酸盐存在下受到紫外光时裂解，表明这两种蛋白质都是动力蛋白HC。针对18 S HC之一的抗体不识别22 S动力蛋白HC。22 S动力蛋白HC的抗体不与18 S动力蛋白光裂解片段明显结合。综上所述，这些结果表明，在18 S处沉积的大蛋白质是轴丝动力蛋白重链。
Two dyneins can be extracted fromTetrahymenaciliary axonemes. The 22S dynein contains three heavy chains (HC), sediments at 22S in a sucrose gradient, and makes up the outer arms. The 14S dynein contains two to six HCs, sediments at 14S, and is thought to contribute to formation of the inner arms. We have identified two large proteins that are extracted fromTetrahymenaaxonemes with high salt and that sediment together at approximately 18S. The two large proteins cleave when subjected to UV light in the presence of ATP and vanadate, suggesting both proteins are dynein HC. Antibodies against one of the 18S HCs do not recognize 22S dynein HCs. Antibodies to 22S dynein HC do not bind appreciably to 18S dynein photocleavage fragments. Taken together, these results indicate that the large proteins that sediment at 18S are axonemal dynein heavy chains.