Domain mobility in proteins: functional and evolutionary implications
Domain mobility in proteins: functional and evolutionary implications
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DOI：
10.1093/bib/bbn057
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发表时间：
2009-05-01
影响因子：
9.5
通讯作者：
Rogozin, Igor B.
中科院分区：
文献类型：
--
作者：
Basu, Malay Kumar;Poliakov, Eugenia;Rogozin, Igor B.
真核生物蛋白质中有相当一部分含有多个结构域，其中一些结构域有出现在不同结构域中的趋势，可以被认为是可移动的(或混杂的)。这些杂乱的结构域通常参与蛋白质的相互作用，并在相互作用网络中发挥关键作用，特别是那些有助于信号转导的网络。它们还在蛋白质组中创造多样化的蛋白质结构域中发挥着重要作用。现在很明显，混杂在进化中是一个不稳定和相对快速变化的特征，并且在整个进化过程中只有几个域保持它们的混杂地位。许多这样的领域在不同的谱系中独立地获得了它们的混杂地位。直到最近，我们才开始了解蛋白质结构域的多样性以及混杂结构域在这种多样性的进化中所起的作用。然而，蛋白质结构域移动性的许多生物学机制仍然是个谜。在这篇综述中，我们讨论了我们目前对蛋白质结构域混杂的理解，它的进化以及它在细胞功能中的作用。
A substantial fraction of eukaryotic proteins contains multiple domains, some of which show a tendency to occur in diverse domain architectures and can be considered mobile (or promiscuous). These promiscuous domains are typically involved in proteinprotein interactions and play crucial roles in interaction networks, particularly those contributing to signal transduction. They also play a major role in creating diversity of protein domain architecture in the proteome. It is now apparent that promiscuity is a volatile and relatively fast-changing feature in evolution, and that only a few domains retain their promiscuity status throughout evolution. Many such domains attained their promiscuity status independently in different lineages. Only recently, we have begun to understand the diversity of protein domain architectures and the role the promiscuous domains play in evolution of this diversity. However, many of the biological mechanisms of protein domain mobility remain shrouded in mystery. In this review, we discuss our present understanding of protein domain promiscuity, its evolution and its role in cellular function.