The ADF homology (ADF-H) domain: A highly exploited actin-binding module
The ADF homology (ADF-H) domain: A highly exploited actin-binding module
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DOI：
10.1091/mbc.9.8.1951
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发表时间：
1998-08-01
影响因子：
3.3
通讯作者：
Drubin, DG
中科院分区：
文献类型：
--
作者：
Lappalainen, P;Kessels, MM;Drubin, DG
基因组测序项目极大地增加了公共数据库中可用的序列数据量，为鉴定新的蛋白质家族提供了机会。新蛋白质家族的定义允许从研究蛋白质家族的一个或几个成员的知识应用于家族中的许多其他蛋白质。本文的分析定义了一个肌动蛋白结合模块，即肌动蛋白解聚因子同源结构域（ADF-H），它存在于一个新发现的广泛蛋白质家族的每个成员中。这个家族由三个系统发育上不同的类别组成：ADF/cofilins， twinfilins和drebrin/Abp1s。在真菌和动物分化之前，每一类都被真核生物使用了超过10亿年。ADF-H结构域可以被认为是一个功能构建块，它在家族中三种蛋白质类别中的每一种中都有不同的排列。除了在进化上可区分之外，每一类蛋白质似乎都具有不同的生化特性。因此，ADF-H结构域的古老复制允许功能多样性的发展。
Genome sequencing projects have dramatically increased the amount of sequence data available in public databases, providing an opportunity to identify new protein families. The definition of new protein families allows knowledge from studies of one or a few members of a protein family to be applied to many other proteins in the family. The analysis presented here defines an actin-binding module, the actin-depolymerizing factor homology (ADF-H) domain, which is present in each member of a newly identified, extensive protein family. This family consists of three phylogenetically distinct classes: the ADF/cofilins, the twinfilins, and the drebrin/Abp1s. Each class has been used by eukaryotic organisms for more than 1 billion years, since before the divergence of fungi and animals. The ADF-H domain can be considered a functional building block that is arranged differently in each of the three protein classes in the family. In addition to being evolutionarily distinguishable, proteins in each class seem to possess distinct biochemical properties. Thus, ancient duplication of the ADF-H domain allowed the development of functional diversity.