Thompson Reid F, Langford George M
Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755, USA.
Anat Rec. 2002 Nov 1;268(3):276-89. doi: 10.1002/ar.10160.
The superfamily of myosin proteins found in eukaryotic cells is known to contain at least 18 different classes. Members are classified based on the phylogenetic analysis of the head domains located at the amino terminus of the polypeptide. While phylogenetic relationships provide insights into the functional relatedness of myosins within and between families, the evolutionary history of the myosin superfamily is not revealed by such studies. In order to establish the evolutionary history of the superfamily, we analyzed the representation of myosin gene families in a range of organisms covering the taxonomic spectrum. The amino acid sequences of 232 myosin heavy chains, as well as 65 organisms representing the protist, plant, and animal kingdoms, were included in this study. A phylogenetic tree of organisms was constructed based on several complementary taxonomic classification schemes. The results of the analysis support an evolutionary hypothesis in which myosins II and I evolved the earliest of all the myosin groups. Myosins V and XI evolved from a common myosin II-like ancestor, but the two families diverged to either the plant (XI) or animal (V) lineage. Class VII myosin appeared fourth among the families, and classes VI and IX appeared later during the early period of metazoan radiation. Myosins III, XV, and XVIII appeared after this group, and X appeared during the formative phases of vertebrate evolution. The remaining members of the myosin superfamily (IV, VI, XII, XIII, XIV, XVI, and XVII) are limited in distribution to one or more groups of organisms. The evolutionary data permits one to predict the likelihood that myosin genes absent from a given species are either missing (not found yet because of insufficient data) or lost due to a mutation that removed the gene from an organism's lineage. In conclusion, an analysis of the evolutionary history of the myosin superfamily suggests that early-appearing myosin families function as generalists, carrying out a number of functions in a variety of cell types, while more recently evolved myosin families function as specialists and are limited to a few organisms or a few cell types within organisms.
真核细胞中发现的肌球蛋白蛋白超家族已知至少包含18个不同的类别。成员是根据位于多肽氨基末端的头部结构域的系统发育分析来分类的。虽然系统发育关系为肌球蛋白在家族内部和家族之间的功能相关性提供了见解,但此类研究并未揭示肌球蛋白超家族的进化历史。为了确定超家族的进化历史,我们分析了一系列涵盖分类谱系的生物体中肌球蛋白基因家族的表现。本研究纳入了232条肌球蛋白重链的氨基酸序列,以及代表原生生物、植物和动物界的65种生物体。基于几种互补的分类方案构建了生物体的系统发育树。分析结果支持一种进化假说,即肌球蛋白II和I是所有肌球蛋白组中最早进化的。肌球蛋白V和XI从一个共同的类肌球蛋白II祖先进化而来,但这两个家族分别分化到植物(XI)或动物(V)谱系。VII类肌球蛋白在各家族中第四个出现,VI和IX类肌球蛋白在后生动物辐射早期较晚出现。肌球蛋白III、XV和XVIII在这一组之后出现,X在脊椎动物进化的形成阶段出现。肌球蛋白超家族的其余成员(IV、VI、XII、XIII、XIV、XVI和XVII)分布局限于一个或多个生物体群体。进化数据使人们能够预测给定物种中缺失的肌球蛋白基因是缺失(由于数据不足尚未发现)还是由于使该基因从生物体谱系中消失的突变而丢失。总之,对肌球蛋白超家族进化历史的分析表明,早期出现的肌球蛋白家族起着多面手的作用,在多种细胞类型中执行多种功能,而最近进化的肌球蛋白家族则起着专家的作用,局限于少数生物体或生物体中的少数细胞类型。