ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein
ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein
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DOI：
10.1038/nsmb930
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发表时间：
2005-06-01
影响因子：
16.8
通讯作者：
Sutoh, K
中科院分区：
文献类型：
--
作者：
Kon, T;Mogami, T;Sutoh, K
据预测，运动蛋白dynein会移动尾部结构域，这是一种细长的杆状结构，相对于催化头部结构域进行其动力行程。在这里，我们利用两个荧光蛋白标记的动力蛋白运动域的荧光共振能量转移分析来研究动力蛋白的依赖于ATP水解周期的构象动力学。我们发现，动力蛋白至少有两种构象状态(状态I和状态II)，在这两种状态之间的转换过程中，尾巴相对于头部结构域经历了ATP诱导的运动。我们的测量还表明，在动力蛋白的ATP水解循环过程中，从状态I到状态II的尾部运动发生在ATP结合的状态，而从状态II到状态I的运动发生在ADP结合的状态。后者的尾部运动可能对应于动力蛋白的预测功率行程。
The motor protein dynein is predicted to move the tail domain, a slender rod-like structure, relative to the catalytic head domain to carry out its power stroke. Here, we investigated ATP hydrolysis cycle-dependent conformational dynamics of dynein using fluorescence resonance energy transfer analysis of the dynein motor domain labeled with two fluorescent proteins. We show that dynein adopts at least two conformational states (states I and II), and the tail undergoes ATP-induced motions relative to the head domain during transitions between the two states. Our measurements also suggest that in the course of the ATP hydrolysis cycle of dynein, the tail motion from state I to state II takes place in the ATP-bound state, whereas the motion from state II to state I occurs in the ADP-bound state. The latter tail motion may correspond to the predicted power stroke of dynein.