Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein
Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein
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DOI：
10.1016/s0014-5793(04)00278-9
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发表时间：
2004-04-09
期刊：
影响因子：
3.5
通讯作者：
Kamiya, R
中科院分区：
文献类型：
--
作者：
Kikushima, K;Yagi, T;Kamiya, R
动力蛋白有四个核苷酸结合位点，除单个催化位点外，其功能意义尚不清楚。为了获得非催化核苷酸结合功能的线索，我们检测了ADP对衣藻内臂动力蛋白物种a的体外运动的影响。连续灌注ATP和ADP后，微管在涂有动力蛋白的玻璃表面上滑动，其速度在几分钟内逐渐增加。ADP浓度越高，速度越快。这些结果表明，这种动力蛋白是通过一个极其缓慢的过程通过核苷酸结合到调节位点而激活的。(C) 2004年由Elsevier B.V.代表欧洲生化学会联合会出版。
Dynein has four nucleotide binding sites, of which the functional significance is unknown except for the single catalytic site. To obtain clues to the function of non-catalytic nucleotide binding, we examined the effect of ADP on the in vitro motility of Chlamydomonas inner-arm dynein species 'a'. Upon continuous perfusion with ATP and ADP, microtubules glided on a dynein-coated glass surface with a velocity that gradually increased over a few minutes. The velocity increased faster at higher ADP concentrations. These results suggest that this dynein is activated by nucleotide binding to regulatory site(s) through an extremely slow process. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.