The tetrameric molecule of conventional kinesin contains identical light chains
The tetrameric molecule of conventional kinesin contains identical light chains
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DOI：
10.1021/bi049288l
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发表时间：
2004-10-26
期刊：
影响因子：
2.9
通讯作者：
Minin, AA
中科院分区：
文献类型：
--
作者：
Gyoeva, FK;Sarkisov, DV;Minin, AA
传统的动蛋白是一种多功能的运动蛋白，可以沿着微管运输许多细胞器。运动蛋白-货物结合的特异性被认为取决于运动蛋白分子所包含的轻链的类型(S)。我们以前已经证明，不同形式的运动蛋白轻链与不同类型的货物、线粒体和高尔基复合体的膜有关。在这里，我们提供了证据，证明存在于每个动蛋白分子中的两个轻链总是属于同一类型。进一步，我们证明了运动蛋白重链与核糖体上新生的轻链多肽相互作用。这些数据表明，两个相同的轻链结合到一个单一的动蛋白分子中很可能是共翻译发生的。
Conventional kinesin is a multifunctional motor protein that transports numerous organelles along microtubules. The specificity of kinesin-cargo binding is thought to depend on the type(s) of light chains that a kinesin molecule contains. We have shown previously that different isoforms of kinesin light chains are associated with different types of cargo, mitochondria and membranes of the Golgi complex. Here, we provide evidence that the two light chains present within each kinesin molecule are always of the same type. Further, we demonstrate that kinesin heavy chains interact with nascent light-chain polypeptides on ribosomes. These data suggest that incorporation of the two identical light chains into a single kinesin molecule most likely occurs cotranslationally.