H结构域及侧翼序列参与AtKP2与微丝的结合
he CH domain and its flanking sequence are involved in the microfilament-binding of AtKP2
动蛋白是真核生物中广泛存在的依赖于微管的马达蛋白。然而，在动蛋白-14家族中却存在这样一类植物特有的动蛋白，它们的N末端含有一个可能参与微丝结合的CH结构域。本实验室从拟南芥中克隆得到的动蛋白AtKP2就是其中之一。研究含有CH结构域的动蛋白与微管和微丝的相互作用，对揭示这类动蛋白的功能具有重要的理论意义。 本实验对AtKP2与微丝的结合机理进行研究。构建了不同长度的N端截短蛋白，将这些截短蛋白融合GFP后在拟南芥原生质体内进行了瞬时表达。实验结果表明，AtKP2的CH结构域具有微丝结合能力，另外，位于CH结构域两侧的1-45位氨基酸残基和200-374位氨基酸残基对其微丝结合能力也有重要作用；CH结构域是拟南芥动蛋白AtKP2 N端结合微丝的必要非充分条件。
Kinesins were widespread microtubule-based motors. However, in kinesin-14 family, a group of plant-specific kinesins contains a single CH (calponin homology) domain at their N-terminus, which was thought to be involved in actin binding in many actin-binding proteins. AtKP2, a kind of CH domain-containing kinesin, was cloned from Arabidopsis thaliana in our laboratory. Working on the interactions between CH domain-containing-kinesins and microfilaments is important for revealing the functions of these kinesins.. In this paper, we try to find the interaction mechanisms between AtKP2 and microfilaments. A series of CH domain-containing N-terminal truncated fragments of AtKP2 were constructed and analyzed. Via in vivo transient overexpression, we found that AtKP2 was capable of binding to microfilaments. Studies revealed that its CH domain played an important role in actin binding, residues 1-45 and 200-374 outside CH domain also contribute to actin binding of AtKP2. CH domain is necessary but not sufficient for the interaction between AtKP2 and microfilaments.
刘国琴、潘晓迪、陈子溦、秦兴华
细胞生物学分子生物学植物学
动蛋白H结构域微丝
kinesinCH domainmicrofilaments
刘国琴,潘晓迪,陈子溦,秦兴华.H结构域及侧翼序列参与AtKP2与微丝的结合[EB/OL].(2012-02-28)[2025-08-11].http://www.paper.edu.cn/releasepaper/content/201202-1099.点此复制
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