Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding.
Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding.
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DOI：
10.1038/nsmb.1555
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发表时间：
2009-03
影响因子：
16.8
通讯作者：
中科院分区：
文献类型：
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atp酶和轨道结合位点之间的耦合是分子马达沿着细胞骨架轨道运动的必要条件。在动力蛋白中，这些位点由一根长卷曲的螺旋状茎分开，该茎必须介导它们之间的通信，但潜在的机制尚不清楚。在这里，我们表明，在注册的两个螺旋之间的线圈线圈可以执行此功能的变化。我们在三个特定的配位上锁定了螺旋状的线圈，将配对半胱氨酸残基的二硫化物氧化引入到两个螺旋中。这些捕获的atp酶活性处于与微管无关的高或低状态，微管结合活性处于atp不敏感的强或弱状态，这取决于盘绕线圈的注册表。我们的研究结果提供了直接证据，表明动力蛋白在其机械化学循环中利用茎的两个螺旋之间的滑动来耦合atp酶和微管结合活性。
Coupling between ATPase and track-binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled-coil stalk which must mediate communication between them, yet the underlying mechanism remains unclear. Here we show that changes in registration between the two helices of the coiled coil can perform this function. We locked the coiled coil at three specific registrations using oxidation to disulfides of paired cysteine residues introduced into the two helices. These trapped ATPase activity either in a microtubule-independent high or low state, and microtubule-binding activity either in an ATP-insensitive strong or weak state, depending on the registry of the coiled coil. Our results provide direct evidence that dynein uses sliding between the two helices of the stalk to couple ATPase and microtubule-binding activities during its mechanochemical cycle.
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DOI：
10.1126/science.1164424
发表时间：
2008-12-12
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Carter AP;Garbarino JE;Wilson-Kubalek EM;Shipley WE;Cho C;Milligan RA;Vale RD;Gibbons IR
通讯作者：
Gibbons IR
影响因子：
3
作者：
Burgess, SA;Walker, ML;Knight, PJ
通讯作者：
Knight, PJ
影响因子：
4.8
作者：
Gibbons, IR;Garbarino, JE;Carter, AP
通讯作者：
Carter, AP
DOI：
10.1073/pnas.0706443104
发表时间：
2007-11-20
影响因子：
11.1
作者：
Arora, Karunesh;Brooks, Charles L., III
通讯作者：
Brooks, Charles L., III
影响因子：
56.9
作者：
GIBBONS, IR;ROWE, AJ
通讯作者：
ROWE, AJ