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Effect of ADP on binding of skeletal S1 to F-actin

机译：ADP对骨骼肌S1与F-肌动蛋白结合的影响

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The proximity of skeletal myosin subfragment-l (S1) to actin, and its orientation with respect to thin filaments of single muscle fibers, were compared in the presence and in the absence of ADP. The proximity was assessed by the efficiency of carbodiimide-induced cross-linking and the orientation by polarization of fluorescence of probes attached to the essential light chains. ADP made no difference in proximity or orientation when the molar ratio of S1 to actin was low or high. However, at the intermediate ratios, ADP made a significant difference. Strong dissociating agents, AMP-PNP and PPI, made significant differences at all ratios. To explain this behavior, it is unnecessary to invoke the ADP-induced "swinging" of the tail of S1. Rather, it is simply explained by the "two-state" model which we proposed earlier, in which S1 binds to one or to two actin protomers, depending on the saturation of the filaments with Sis. The dissociation induced by the ADP shifts the equilibrium between the two bound states. At high and low degrees of saturation, ADP is unable to significantly decrease the amount of S1 bound to F-actin. However, at intermediate saturation levels, ADP causes significantly more Sis to bind to two actins. These results suggest that the ADP-induced changes seen at the intermediate molar ratios are due to the dissociation-induced reorientation of S1. [References: 43]
机译：在有和没有ADP的情况下，比较了骨骼肌肌球蛋白亚片段-1（S1）与肌动蛋白的接近程度，以及其相对于单条肌纤维细丝的取向。通过碳二亚胺诱导的交联效率和通过附着在基本轻链上的探针的荧光偏振确定取向来评估邻近性。当S1与肌动蛋白的摩尔比低或高时，ADP在接近度或取向上没有差异。但是，在中间比率下，ADP产生了显着差异。强解离剂AMP-PNP和PPI在所有比例下均具有显着差异。为了解释此行为，没有必要调用ADP引起的S1尾部的“摆动”。相反，它是由我们先前提出的“两种状态”模型简单解释的，其中S1结合到一个或两个肌动蛋白启动子上，这取决于细丝的Si饱和度。 ADP引起的离解改变了两个结合态之间的平衡。在高和低饱和度下，ADP无法显着减少与F-肌动蛋白结合的S1的量。但是，在中等饱和水平，ADP会导致更多的Si与两个肌动蛋白结合。这些结果表明，在中等摩尔比下，ADP引起的变化是由于S1的解离引起的重新取向。 [参考：43]

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