Identification and phylogenetic analysis of Drosophila melanogaster myosins.

Identification and phylogenetic analysis of Drosophila melanogaster myosins.
复制标题

DOI:
10.1093/oxfordjournals.molbev.a004163
复制
发表时间:
2002-07
影响因子:
10.7
通讯作者:
G. Tzolovsky;Hadas Millo;S. Pathirana;T. Wood;M. Bownes
G. Tzolovsky;Hadas Millo;S. Pathirana;T. Wood;M. Bownes
中科院分区:
生物学1区
文献类型:
--
作者:
G. Tzolovsky;Hadas Millo;S. Pathirana;T. Wood;M. Bownes

文献摘要

被引文献

相似文献

肌球蛋白构成了运动蛋白超家族,可将 ATP 水解产生的能量转化为沿肌动蛋白丝的机械运动。目前,系统发育分析根据肌球蛋白保守运动域的类别特异性特征将其分为 17 个类别。传统上,肌球蛋白根据它们是否形成单体或二聚体分为两类。肌肉和非肌肉细胞的常规肌球蛋白形成II类肌球蛋白。它们是由四条轻链与两条重链结合而成的复杂分子,通过卷曲螺旋尾部之间的相互作用形成双极丝(II 型)。 I 类肌球蛋白是较小的单体肌球蛋白,称为非常规肌球蛋白。现在,至少有 15 种其他类型的非常规肌球蛋白是已知的。需要多少肌球蛋白才能确保真核生物的正常发育和功能?迄今为止,在芽殖酵母中发现了 3 种肌球蛋白,在线虫中发现了 6 种肌球蛋白,在人类中发现了至少 12 种肌球蛋白。在这里,我们报告了果蝇肌球蛋白的鉴定和分类。对果蝇基因组序列的分析确定了 13 个肌球蛋白基因。基于肌球蛋白运动结构域的序列比较以及类特异性结构域的存在的系统发育分析表明,果蝇肌球蛋白可分为九个主要类。存在属于前述 I、II、III、V、VI 和 VII 类的肌球蛋白。分子和系统发育分析表明,果蝇基因组至少含有五种新的肌球蛋白。其中三个属于先前描述的肌球蛋白 I、VII 和 XV 类。另一种肌球蛋白是小鼠和人类含有 PDZ 的肌球蛋白的同源物,形成最近定义的 XVIII 类肌球蛋白。 PDZ 结构域以突触后密度、圆盘大、ZO-1 蛋白命名,它们是在其中首次描述的。第五种肌球蛋白显示出独特的结构域组成以及与任何现有类别的低同源性。我们建议当在其他物种中发现类似的肌球蛋白时对其进行分类。
Myosins constitute a superfamily of motor proteins that convert energy from ATP hydrolysis into mechanical movement along the actin filaments. Phylogenetic analysis currently places myosins into 17 classes based on class-specific features of their conserved motor domain. Traditionally, the myosins have been divided into two classes depending on whether they form monomers or dimers. The conventional myosin of muscle and nonmuscle cells forms class II myosins. They are complex molecules of four light chains bound to two heavy chains that form bipolar filaments via interactions between their coiled-coil tails (type II). Class I myosins are smaller monomeric myosins referred to as unconventional myosins. Now, at least 15 other classes of unconventional myosins are known. How many myosins are needed to ensure the proper development and function of eukaryotic organisms? Thus far, three types of myosins were found in budding yeast, six in the nematode Caenorhabditis elegans, and at least 12 in human. Here, we report on the identification and classification of Drosophila melanogaster myosins. Analysis of the Drosophila genome sequence identified 13 myosin genes. Phylogenetic analysis based on the sequence comparison of the myosin motor domains, as well as the presence of the class-specific domains, suggests that Drosophila myosins can be divided into nine major classes. Myosins belonging to previously described classes I, II, III, V, VI, and VII are present. Molecular and phylogenetic analysis indicates that the fruitfly genome contains at least five new myosins. Three of them fall into previously described myosin classes I, VII, and XV. Another myosin is a homolog of the mouse and human PDZ-containing myosins, forming the recently defined class XVIII myosins. PDZ domains are named after the postsynaptic density, disc-large, ZO-1 proteins in which they were first described. The fifth myosin shows a unique domain composition and a low homology to any of the existing classes. We propose that this is classified when similar myosins are identified in other species.