Association between actin and light chains in Chlamydomonas flagellar inner-arm dyneins
Association between actin and light chains in Chlamydomonas flagellar inner-arm dyneins
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DOI：
10.1006/bbrc.2001.5776
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发表时间：
2001-10-26
影响因子：
3.1
通讯作者：
Kamiya, R
中科院分区：
文献类型：
--
作者：
Yanagisawa, H;Kamiya, R
纤毛和鞭毛中的内部动力蛋白臂含有肌动蛋白作为亚基，然而，这种肌动蛋白的功能是完全未知的。在这里，我们进行了化学交联实验，以检查肌动蛋白与其他亚基的相互作用。六的七个衣原体内臂动力蛋白物种分离阴离子交换色谱含有肌动蛋白和，任何一个先前确定的两个轻链，p28和中心蛋白，在一个相互排斥的方式。化学交联动力蛋白的Western印迹表明，肌动蛋白是直接与p28和中心蛋白，但不与动力蛋白重链（HC）。相比之下，p28和centrin似乎都直接与HC的N-末端一半相互作用。因此，肌动蛋白可能通过p28/中心蛋白与重链结合。这些轻链可以很好地在组装或靶向内臂到正确的轴丝位置中起作用。(C)北京：科学出版社.
Inner dynein arms in cilia and flagella contain actin as a subunit; however, the function of this actin is totally unknown. Here we performed chemical crosslinking experiments to examine the interaction of actin with other subunits. Six of the seven Chlamydomonas inner-arm dynein species separated by anion-exchange chromatography contain actin and, either one of the two previously identified light chains, p28 and centrin, in a mutually exclusive manner. Western blotting of chemically crosslinked dyneins indicated that actin is directly associated with p28 and centrin but not with the dynein heavy chains (HCs). In contrast, p28 and centrin both appeared to interact directly with the N-terminal half of the HCs. Thus it is likely that actin is associated with the heavy chains through p28/centrin. These light chains may well function in the assembly or targeting of the inner arm to the correct axonemal location. (C) 2001 Academic Press.