Unravelling the Properties of Single a-Helical Domains in Myosin and other Proteins
Unravelling the Properties of Single a-Helical Domains in Myosin and other Proteins
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揭示肌球蛋白和其他蛋白质中单个α螺旋结构域的特性
DOI：
10.1016/j.bpj.2013.11.3459
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发表时间：
2014
影响因子：
3.4
通讯作者：
Wolny M
中科院分区：
文献类型：
--
作者：
Wolny M
在大多数蛋白质中，α-螺旋通过与相邻二级结构元件（如卷曲螺旋）的相互作用而稳定。然而，我们最近发现，许多蛋白质含有单一的α-螺旋（SAH）结构域，这是稳定的分离和通常插入两个不同的功能域之间。SAH结构域富含精氨酸、赖氨酸和谷氨酸残基。它们的稳定性来自R和E或K和E之间的许多潜在的（i，i±4）和（i，i±3）螺旋内相互作用。迄今为止，研究最多的SAH结构域是来自肌球蛋白6和10以及网骨藻肌球蛋白myoM的结构域，它们可能形成功能杠杆的一部分。也预测肌球蛋白7a的SAH结构域。我们已经证明，SAH结构域可以在功能上取代肌球蛋白5a的典型杠杆在体外。在细胞中，失去SAH结构域的肌球蛋白10仍然移动到丝状伪足的尖端，但速度降低。
In most proteins, α-helices are stabilised by interactions with neighbouring secondary structure elements (eg coiled-coils). However, we recently showed that many proteins contain single α-helical (SAH) domains, which are stable in isolation and commonly inserted between two different functional domains. SAH domains are rich in arginine, lysine and glutamic acid residues. Their stability arises from the many potential (i, i±4) and (i, i±3) intrahelical interactions between either R and E, or K and E.To date, the best-studied SAH domains are those from myosins 6 and 10, and the Dictyostelium myosin myoM, where they are likely to form part of the functional lever. A SAH domain is also predicted for myosin 7a. We have shown that the SAH domain can functionally substitute for the canonical lever in myosin 5a in vitro. In cells, myosin 10 missing its SAH domain still moves to the tips of filopodia but with a reduced velocity.