Goodson H V, Spudich J A
Department of Biochemistry, Beckman Center for Molecular and Genetic Medicine, Stanford University Medical School, CA 94305.
Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):659-63. doi: 10.1073/pnas.90.2.659.
To examine the evolutionary relationships between members of the myosin family, we have used two different phylogenetic methods, distance matrix and maximum parsimony, to analyze all available myosin head sequences. We find that there are at least three equally divergent classes of myosin, demonstrating that the current classification of myosin into only two classes needs to be reexamined. In the myosin II class, smooth muscle myosin is more closely related to nonmuscle myosin than to striated muscle myosin, implying that smooth muscle and skeletal muscle myosins were independently derived from nonmuscle myosin and suggesting that similarities between these types of muscle are the result of convergent evolution. The grouping of head sequences produced by phylogenetic analysis is consistent with classifications based on enzymology and structural localization and is generally consistent with grouping based on common tail structure elements. This result demonstrates that specific head sequences are tightly coupled to specific tail sequences throughout evolution and challenges the idea that myosin heads are freely interchangeable units whose unique function is determined only by the tail structure to which it is attached.
为了研究肌球蛋白家族成员之间的进化关系,我们使用了两种不同的系统发育方法,即距离矩阵法和最大简约法,来分析所有可用的肌球蛋白头部序列。我们发现,肌球蛋白至少有三个同等分化的类别,这表明目前仅将肌球蛋白分为两类的分类方式需要重新审视。在肌球蛋白II类中,平滑肌肌球蛋白与非肌肉肌球蛋白的关系比与横纹肌肌球蛋白的关系更为密切,这意味着平滑肌和骨骼肌肌球蛋白是独立地从非肌肉肌球蛋白衍生而来的,并表明这些类型肌肉之间的相似性是趋同进化的结果。系统发育分析产生的头部序列分组与基于酶学和结构定位的分类一致,并且通常与基于共同尾部结构元件的分组一致。这一结果表明,在整个进化过程中,特定的头部序列与特定的尾部序列紧密相连,并且挑战了肌球蛋白头部是可自由互换的单元,其独特功能仅由其所连接的尾部结构决定的观点。