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首页> 外文期刊>Journal of Molecular Biology >Filament Assembly by Spire: Key Residues and Concerted Actin Binding
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Filament Assembly by Spire: Key Residues and Concerted Actin Binding

机译：Spire的细丝装配：主要残基和协同的肌动蛋白结合

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摘要

The most recently identified class of actin nucleators, WASp homology domain 2 (WH2) nucleators, use tandem repeats of monomeric actin-binding WH2 domains to facilitate actin nucleation. WH2 domains are involved in a wide variety of actin regulatory activities. Structurally, they are expected to clash with interprotomer contacts within the actin filament. Thus, the discovery of their role in nucleation was surprising. Here we use Drosophila Spire (Spir) as a model system to investigate both how tandem WH2 domains can nucleate actin and what differentiates nucleating WH2-containing proteins from their non-nucleating counterparts. We found that the third WH2 domain in Spir (Spir-C or Sc) plays a unique role. In the context of a short nucleation construct (containing only two WH2 domains), placement of Sc in the N-terminal position was required for the most potent nucleation. We found that the native organization of the WH2 domains with respect to each other is necessary for binding to actin with positive cooperativity. We identified two residues within Sc that are critical for its activity. Using this information, we were able to convert a weak synthetic nucleator into one with activity equal to a native Spir construct. Lastly, we found evidence that Sc binds actin filaments, in addition to monomers. (C) 2014 Elsevier Ltd. All rights reserved.
机译：WASp同源域2（WH2）成核剂是最近鉴定出的肌动蛋白成核剂类别，它使用单体肌动蛋白结合WH2域的串联重复序列来促进肌动蛋白成核。 WH2域参与多种肌动蛋白调节活动。从结构上讲，它们有望与肌动蛋白丝内的protomtomer接触发生冲突。因此，发现它们在成核中的作用是令人惊讶的。在这里，我们使用果蝇尖峰（Spir）作为模型系统，以研究串联WH2域如何使肌动蛋白成核，以及使含WH2的成核蛋白与非成核的对应蛋白区别开来。我们发现Spir中的第三个WH2域（Spir-C或Sc）起着独特的作用。在短成核构建体（仅包含两个WH2域）的情况下，最有效的成核需要将Sc置于N端位置。我们发现，WH2域彼此之间的天然组织对于以积极的协同性结合肌动蛋白是必需的。我们确定了Sc中两个对其活性至关重要的残基。利用这些信息，我们能够将弱合成成核剂转化为活性与天然Spir结构相同的成核剂。最后，我们发现有证据表明Sc除单体外还结合肌动蛋白丝。 （C）2014 Elsevier Ltd.保留所有权利。

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