Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the γ heavy chain
Light chain 1 from the Chlamydomonas outer dynein arm is a leucine-rich repeat protein associated with the motor domain of the γ heavy chain
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DOI：
10.1021/bi990466y
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发表时间：
1999-06-01
期刊：
影响因子：
2.9
通讯作者：
King, SM
中科院分区：
文献类型：
--
作者：
Benashski, SE;Patel-King, RS;King, SM
来自衣藻外臂动力蛋白的 LC1 轻链与 γ 重链紧密结合。分子克隆表明，LC1 是富含亮氨酸重复蛋白家族的 SDS22+ 亚类的成员，因此可能参与介导动力蛋白与信号转导途径组件之间的相互作用。通过共价交联和钒酸盐介导的光解作用的结合，发现 LC1 与 P1 环 C 端的 γ HC 部分结合。该区域包含重链的大部分球状头结构域，并包括参与微管结合的茎状结构。 LC1 与该区域的连接代表了与动力蛋白运动结构域直接相关的附加多肽的唯一已知例子。其他交联实验表明，LC1 还可以直接与类似 45 kDa 轴丝成分原位相互作用；这种相互作用被用于从轴丝上去除外臂的标准高盐处理所破坏。这些数据表明 LC1 的作用是介导该 45 kDa 轴丝多肽与 γ HC 运动单位之间的关联。
The LC1 light chain from Chlamydomonas outer arm dynein is tightly bound to the gamma heavy chain. Molecular cloning revealed that LC1 is a member of the SDS22+ subclass of the leucine-rich repeat protein family and as such is likely involved in mediating interactions between dynein and the components of a signal transduction pathway. Through the combination of covalent cross-linking and vanadate-mediated photolysis, LC1 was found to associate with that portion of the gamma HC that is C-terminal to the P1 loop. This region comprises most of the globular head domain of the heavy chain and includes the stalk-like structure that is involved in microtubule binding. Attachment of LC1 to this region represents the only known example of an accessory polypeptide directly associated with a dynein motor domain. Additional cross-linking experiments revealed that LC1 also interacts directly in situ with an similar to 45 kDa axonemal component; this interaction is disrupted by the standard high salt treatment used to remove the outer arm from the axoneme. These data suggest that LC1 acts to mediate the association between this 45 kDa axonemal polypeptide and the motor unit of the gamma HC.