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Autonomous and in Trans functions for the two halves of Srv2/CAP in promoting actin turnover

机译：Srv2 / CAP的两半的自主和In Trans功能促进肌动蛋白更新

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Recent evidence has suggested that Srv2/CAP (cyclase-associated protein) has two distinct functional roles in regulating actin turnover, with its N-terminus enhancing cofilin-mediated severing of actin filaments and its C-terminus catalyzing actin monomer recycling. However, it has remained unclear to what degree these two activities are coordinated by being linked in one molecule, or whether they can function autonomously. To address this, we physically divided the protein into two separate halves, N-Srv2 and C-Srv2, and asked whether they are able to function in trans both in living cells and in reconstituted assays for F-actin turnover and actin-based motility. Remarkably, in F-actin turnover assays the stimulatory effects of N-Srv2 and C-Srv2 functioning in trans were quantitatively similar to those of intact full-length Srv2. Further, in bead motility assays and in vivo, the fragments again functioned in trans, although not with the full effectiveness of intact Srv2. From these data, we conclude that the functions of the two halves of Srv2/CAP are largely autonomous, although their linkage improves coordination of the two functions in specific settings, possibly explaining why the linkage is conserved across distant plant, animal, and fungal species.
机译：最近的证据表明，Srv2 / CAP（环化酶相关蛋白）在调节肌动蛋白周转中具有两个截然不同的功能作用，其N端增强肌动蛋白丝的cofilin介导的切断，其C端催化肌动蛋白单体的循环。但是，尚不清楚这两种活性在一个分子中的连接程度如何，或者它们是否可以自主发挥作用。为了解决这个问题，我们将蛋白质物理上分为两个独立的部分，即N-Srv2和C-Srv2，并询问它们是否能够在活细胞中以及在重组的F-肌动蛋白更新和基于肌动蛋白的运动测定中均具有反式功能。值得注意的是，在F-肌动蛋白更新测定中，N-Srv2和C-Srv2反式功能的刺激作用在数量上与完整全长Srv2相似。此外，在珠子运动性测定中和在体内，该片段再次具有反式功能，尽管并不具有完整Srv2的全部效力。从这些数据中，我们得出结论，Srv2 / CAP的两个半部分的功能在很大程度上是自主的，尽管它们的连接改善了特定环境中两个功能的协调性，这可能解释了为什么在遥远的动植物，真菌和真菌物种中保持这种连接的原因。

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