School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.
Proteins. 2020 Oct;88(10):1361-1375. doi: 10.1002/prot.25955. Epub 2020 Jun 25.
Years of evolution have kept actin conserved throughout various clades of life. It is an essential protein starring in many cellular processes. In a primitive eukaryote named Entamoeba histolytica, actin directs the process of phagocytosis. A finely tuned coordination between various actin-binding proteins (ABPs) choreographs this process and forms one of the virulence factors for this protist pathogen. The ever-expanding world of ABPs always has space to accommodate new and varied types of proteins to the earlier existing repertoire. In this article, we report the identification of 390 ABPs from Entamoeba histolytica. These proteins are part of diverse families that have been known to regulate actin dynamics. Most of the proteins are primarily uncharacterized in this organism; however, this study aims to annotate the ABPs based on their domain arrangements. A unique characteristic about some of the ABPs found is the combination of domains present in them unlike any other reported till date. Calponin domain-containing proteins formed the largest group among all types with 38 proteins, followed by 29 proteins with the infamous BAR domain in them, and 23 proteins belonging to actin-related proteins. The other protein families had a lesser number of members. Presence of exclusive domain arrangements in these proteins could guide us to yet unknown actin regulatory mechanisms prevalent in nature. This article is the first step to unraveling them.
经过多年的进化，肌动蛋白在生命的各个进化枝中都得到了保守。它是一种在许多细胞过程中起重要作用的必需蛋白。在一种名为溶组织内阿米巴的原始真核生物中，肌动蛋白指导吞噬作用的过程。各种肌动蛋白结合蛋白（ABP）之间的精细协调使这个过程协调起来，并形成这个原生动物病原体的毒力因子之一。ABP 的不断扩展的世界总是有空间容纳新的和不同类型的蛋白质到早期存在的库中。在本文中，我们报道了从溶组织内阿米巴中鉴定出的 390 种 ABP。这些蛋白是调节肌动蛋白动力学的不同家族的一部分。这些蛋白中的大多数在该生物中主要是未被表征的；然而，本研究旨在根据它们的结构域排列来注释 ABP。一些发现的 ABP 的一个独特特征是它们所具有的结构域组合与迄今为止报道的任何其他结构域都不同。钙调蛋白结构域蛋白是所有类型中最大的一组，有 38 种蛋白，其次是含有臭名昭著的 BAR 结构域的 29 种蛋白，以及属于肌动蛋白相关蛋白的 23 种蛋白。其他蛋白家族的成员较少。这些蛋白中存在独特的结构域排列，可能指导我们发现自然界中尚未被发现的肌动蛋白调节机制。本文是揭示这些机制的第一步。
