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首页> 外文期刊>Cell motility and the cytoskeleton >Severing of F-actin by yeast cofilin is pH-independent.
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Severing of F-actin by yeast cofilin is pH-independent.

机译：酵母菌纤溶酶切断F-肌动蛋白不依赖pH。

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摘要

Cofilin plays an important role in actin turnover in cells by severing actin filaments and accelerating their depolymerization. The role of pH in the severing by cofilin was examined using fluorescence microscopy. To facilitate the imaging of actin filaments and to avoid the use of rhodamine phalloidin, which competes with cofilin, alpha-actin was labeled with tetramethylrhodamine cadaverine (TRC) at Gln41. The TRC-labeling inhibited actin treadmilling strongly, as measured by epsilonATP release. Cofilin binding, detected via an increase in light scattering, and the subsequent conformational change in filament structure, as detected by TRC fluorescence decay, occurred 2-3 times faster at pH 6.8 than at pH 8.0. In contrast, actin filaments severing by cofilin was pH-independent. The pH-independent severing by cofilin was confirmed using actin labeled at Cys374 with Oregon Green 488 maleimide. The depolymerization of actin by cofilin was faster at high pH.
机译：通过切断肌动蛋白丝并加速其解聚作用，Cofilin在细胞肌动蛋白更新中起着重要作用。使用荧光显微镜检查了pH在cofilin切断中的作用。为了促进肌动蛋白丝的成像并避免使用与cofilin竞争的若丹明鬼笔环肽，在Gln41用四甲基罗丹明尸胺（TRC）标记了α-肌动蛋白。 TRC标记强烈抑制肌动蛋白的跑步，如εATP释放所测量。通过TRC荧光衰减检测到的通过光散射增加检测到的Cofilin结合以及随后的细丝结构构象变化在pH 6.8时比在pH 8.0时快2-3倍。相反，被cofilin切断的肌动蛋白丝不依赖于pH。使用在俄勒冈州格林488马来酰亚胺上标记在Cys374上的肌动蛋白，证实了cofilin的pH依赖性切割。肌动蛋白由cofilin的解聚作用在高pH下更快。

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