Mihashi K, Suzuki N, Ooi A
Department of Physics, Faculty of Science, Nagoya University, Japan.
Biophys Chem. 1989 May;33(2):195-204. doi: 10.1016/0301-4622(89)80021-3.
A novel method that we have developed in the preceding paper to study the subunit exchange rates of F-actin (N. Suzuki and K. Mihashi, Biophys. Chem. 33 (1989) 177) was applied to regulated F-actin (a complex of F-actin, tropomyosin and troponin). We found that the dynamic polarity of regulated F-actin is modulated in a Ca2+-dependent manner, giving rise to strong suppression of the on/off rates of subunit exchange at the P-end. We interpreted this characteristic suppression as follows. Removal of Ca2+ from troponin C in regulated F-actin produces strong constraints on fluctuations in potential energy of an intermediate conformation of the terminal structure (P-end) which would be formed in the course of association and dissociation of the actin subunit.
我们在前一篇论文中开发的一种用于研究F-肌动蛋白亚基交换速率的新方法(N. 铃木和K. 三桥,《生物物理化学》33 (1989) 177)被应用于调节型F-肌动蛋白(F-肌动蛋白、原肌球蛋白和肌钙蛋白的复合物)。我们发现,调节型F-肌动蛋白的动态极性以Ca2+依赖的方式被调节,导致P端亚基交换的开/关速率受到强烈抑制。我们对这种特征性抑制的解释如下。从调节型F-肌动蛋白的肌钙蛋白C中去除Ca2+会对肌动蛋白亚基结合和解离过程中形成的末端结构(P端)中间构象的势能波动产生强烈限制。