兔骨骼肌重酶解肌球蛋白的两个头部在与肌动蛋白结合过程中的协同作用。
Cooperativity between the two heads of rabbit skeletal muscle heavy meromyosin in binding to actin.
作者信息
Conibear P B, Geeves M A
机构信息
Department of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom.
出版信息
Biophys J. 1998 Aug;75(2):926-37. doi: 10.1016/S0006-3495(98)77581-2.
Abstract
An extensive series of experiments in this laboratory has shown that the binding of actin to rabbit skeletal muscle myosin subfragment-1 (a single-headed subfragment) can be described by a two-step model, with formation of a weakly bound complex, the A-state, followed by an isomerization to a more tightly bound complex, the R-state. In this paper, we report on additional experiments comparing the subfragment-1 with heavy meromyosin (a two-headed subfragment). Using a modeling approach, we have quantitated the two-step binding for each of the two heads. This indicates that the binding is cooperative and leads to a more complex view of the acto-myosin interaction than has previously been acknowledged. Implications for the dynamic behavior of the two heads during muscle contraction are discussed.
摘要
本实验室进行的一系列广泛实验表明，肌动蛋白与兔骨骼肌肌球蛋白亚片段-1（单头亚片段）的结合可用两步模型来描述，即先形成弱结合复合物（A态），随后异构化为结合更紧密的复合物（R态）。在本文中，我们报告了将亚片段-1与重酶解肌球蛋白（双头亚片段）进行比较的额外实验。我们采用建模方法，对两个头部各自的两步结合进行了定量。这表明这种结合具有协同性，并且对肌动蛋白-肌球蛋白相互作用的认识比以往所承认的更为复杂。文中还讨论了这对肌肉收缩过程中两个头部动态行为的影响。
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