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首页> 外文期刊>Parasitology >Evolutionary conservation of actin-binding proteins in Trypanosoma cruzi and unusual subcellular localization of the actin homologue.
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Evolutionary conservation of actin-binding proteins in Trypanosoma cruzi and unusual subcellular localization of the actin homologue.

机译：克氏锥虫中肌动蛋白结合蛋白的进化保守性和肌动蛋白同源物的异常亚细胞定位。

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摘要

The actin cytoskeleton controls pivotal cellular processes such as motility and cytokinesis, as well as cell-cell and cell-substrate interactions. Assembly and spatial organization of actin filaments are dynamic events regulated by a large repertoire of actin-binding proteins. This report presents the first detailed characterization of the Trypanosoma cruzi actin (TcActin). Protein sequence analysis and homology modelling revealed that the overall structure of T. cruzi actin is conserved and that the majority of amino-acid changes are concentrated on the monomer surface. Immunofluorescence assays using specific polyclonal antibody against TcActin revealed numerous rounded and punctated structures spread all over the parasitic body. No pattern differences could be found between epimastigotes and trypomastigotes or amastigotes. Moreover, in detergent extracts, TcActin was localized only in the soluble fraction, indicating its presence in the G-actin form or in short filaments dissociated from the microtubule cytoskeleton. The trypanosomatid genome was prospected to identify actin-binding and actin-related conserved proteins. The main proteins responsible for actin nucleation and treadmilling in higher eukaryotes are conserved in T. cruzi.
机译：肌动蛋白的细胞骨架控制关键的细胞过程，例如运动性和胞质分裂，以及细胞-细胞和细胞-底物的相互作用。肌动蛋白丝的组装和空间组织是由肌动蛋白结合蛋白的大量组成调控的动态事件。本报告首次提出了克氏锥虫肌动蛋白（TcActin）的详细表征。蛋白质序列分析和同源性建模表明，克鲁维斯肌动蛋白的整体结构是保守的，大部分氨基酸变化都集中在单体表面。使用针对TcActin的特异性多克隆抗体进行的免疫荧光分析显示，许多圆形和点状结构遍布整个寄生体。在前鞭毛体和锥鞭毛体或变形虫之间没有发现模式差异。此外，在去污剂提取物中，TcActin仅位于可溶级分中，表明它以G-肌动蛋白形式或从微管细胞骨架解离的短丝形式存在。锥虫基因组有望鉴定肌动蛋白结合蛋白和肌动蛋白相关的保守蛋白。在高等真核生物中，负责肌动蛋白成核和跑步的主要蛋白质在克鲁维酵母中是保守的。

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