Coevolution of head, neck, and tail domains of myosin heavy chains
Coevolution of head, neck, and tail domains of myosin heavy chains
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肌球蛋白重链头部、颈部和尾部结构域的共同进化
DOI：
10.1073/pnas.230441597
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发表时间：
2000-11-07
影响因子：
11.1
通讯作者：
Korn, ED
中科院分区：
文献类型：
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作者：
Korn, ED
肌球蛋白是一大类基于肌动蛋白的马达，具有一条或两条重链，每条重链都有一条或多条轻链。重链具有（通常）带有 ATP 酶和肌动蛋白结合位点的 N 端头结构域，随后是轻链结合的颈结构域，以及重链通过其自缔合和/或将肌球蛋白与其货物结合的 C 端尾结构域。肌球蛋白超家族的大约 140 个成员根据其头部结构域的序列分为 17 个类别。我现在展示了基于颈部和尾部组合域序列的系统发育树，将 144 个肌球蛋白（除了少数例外）分为相同的 17 个类。对于具有多个成员的九个肌球蛋白类别，基于头域或组合颈/尾域的系统发育树是相同或非常相似的。对于 II 类肌球蛋白。非常相似的系统发育：获得了 47 条重链、29 条必需轻链和 19 条调节轻链的头、颈和尾部结构域的树。这些数据强烈表明所有肌球蛋白重链的头、颈和尾部结构域。至少 II 类肌球蛋白的轻链和轻链共同进化，并且可能在功能上相互依赖，这与生化证据一致，表明盘基网柄菌肌球蛋白 II 的受调节的肌动蛋白依赖性 MgATP 酶活性需要重链头、尾和轻链之间的亚型特异性相互作用。
Myosins, a large family of actin-based motors, have one or two heavy chains with one or more light chains associated with each heavy chain. The heavy chains have a (generally) N-terminal head domain with an ATPase and actin-binding site, followed by a neck domain to which the light chains bind, and a C-terminal tail domain through which the heavy chains self-associate and/or bind the myosin to its cargo. Approximately 140 members of the myosin superfamily have been grouped into 17 classes based on the sequences of their head domains. I now show that a phylogenetic tree based on the sequences of the combined neck and tail domains groups 144 myosins, with a few exceptions, into the same 17 classes. For the nine myosin classes that have multiple members, phylogenetic trees based on the head domain or the combined neck/tail domains are either identical or very similar. For class II myosins. very similar phylogenetic: trees are obtained for the head, neck, and tail domains of 47 heavy chains and for 29 essential light chains and 19 regulatory light chains. These data strongly suggest that the head, neck, and tail domains of all myosin heavy chains. and light chains at least of class II myosins, have coevolved and are likely to be functionally interdependent, consistent with biochemical evidence showing that regulated actin-dependent MgATPase activity of Dictyostelium myosin II requires isoform specific interactions between the heavy chain head and tail and light chains.