PHYLOGENETIC ANALYSIS OF THE MYOSIN SUPERFAMILY
PHYLOGENETIC ANALYSIS OF THE MYOSIN SUPERFAMILY
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DOI：
10.1002/cm.970240402
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发表时间：
1993-01-01
影响因子：
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通讯作者：
MOOSEKER, MS
中科院分区：
文献类型：
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作者：
CHENEY, RE;RILEY, MA;MOOSEKER, MS
在过去的几年中，已经清楚的是，肌球蛋白构成了一个超家族的蛋白质，其特征在于存在一个保守的80 kDa的马达结构域连接到各种结构上不同的尾部结构域。传统上，肌球蛋白根据它们是否形成单体或二聚体而分为两类。肌球蛋白-I1是常见于肌肉收缩研究中的常规双头且形成双头肌球蛋白的肌球蛋白[综述于Warrick和Spudich，1987 1]，而肌球蛋白-I是最早发现于黑腹蛛属中的较小单体肌球蛋白[Pollard和Korn，1973 1]，但现在已知广泛分布[综述于Pollard等人，1991; Hammer，1991;切尼和Mooseker，19921。最近，新发现的肌球蛋白的数量出现了实质性的爆炸，这已经威胁到将肌球蛋白简单地分为两类。由于它是一个肌球蛋白样的头部结构域的存在，定义了肌球蛋白超家族的成员，我们已经分类肌球蛋白的基础上比较其头部结构域的氨基酸序列。这种方法有几个优点。首先，由于一级序列最终定义了肌球蛋白的身份和结构，因此使用该序列信息来划分类别而不是使用单一的生物化学性质（例如蛋白质是否二聚化）是有意义的。其次，许多非常规肌球蛋白的序列可能在其纯化和生物化学性质（如二聚化）表征之前数年就可获得。最后，基于头部结构域序列的分类应该更准确地反映肌球蛋白之间的系统发育关系，并且系统发育为分类提供了有用的和逻辑的基础。作为定义肌球蛋白超家族的不同类别的初步尝试，我们进行了一个phylo-
Within the last few years it has become clear that the myosins constitute a superfamily of proteins characterized by the presence of a conserved-80 kDa motor domain attached to a variety of structurally distinct tail domains. Traditionally the myosins have been divided into two classes based upon whether they form monomers or dimers. The myosins-I1 are the conventional two-headed and filament-forming myosins familiar from studies of muscle contraction [reviewed in Warrick and Spudich, 19871, while the myosins-I are the smaller monomeric myosins first discovered in Acantharnoeba [Pollard and Korn, 19731, but now known to be widely distributed [reviewed in Pollard et al., 1991; Hammer, 1991; Cheney and Mooseker, 19921. Recently there has been a virtual explosion in the number of newly identified myosins which has threatened to overwhelm the simple division of the myosins into two classes. Since it is the presence of a myosin-like head domain that defines the members of the myosin superfamily, we have classified the myosins based upon a comparison of their head domain amino acid sequences. This approach has several advantages. First, since it is the primary sequence that ultimately defines the identity and structure of a myosin, it makes sense to use this sequence information to delineate classes instead of using a single biochemical property such as whether or not a protein dimerizes. Second, the sequences of many unconventional myosins are likely to be available for years prior to their purification and characterization with respect to biochemical properties such as dimerization. Finally, a classification based upon head domain sequences should more accurately reflect the phylogenetic relationships among myosins, and a phylogeny provides a useful and logical basis for classification. As an initial attempt to define the different classes of the myosin superfamily, we have performed a phylo-