Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.

Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.
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DOI:
10.3390/ijms241512324
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发表时间:
2023-08-01
影响因子:
5.6
通讯作者:
Bianco, Pasquale
Bianco, Pasquale
中科院分区:
生物学2区
文献类型:
--
作者:
Pertici, Irene;Bongini, Lorenzo;Caremani, Marco;Reconditi, Massimo;Linari, Marco;Piazzesi, Gabriella;Lombardi, Vincenzo;Bianco, Pasquale

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脊椎动物骨骼肌在等长和等张收缩过程中的机械性能与相应的能量消耗相结合,以定义肌球蛋白-肌动蛋白能量转导循环中机械和生化步骤之间的耦合。该分析扩展到简化的合成纳米机器,其中从快速哺乳动物骨骼肌中纯化的八个 HMM 分子在 2 mM ATP 存在下与肌动蛋白丝相互作用,以评估在整体中工作的最少数量的马达的新兴特性,而不受横纹肌组织和其他肌节、调节和细胞骨架蛋白的更高层次的影响。肌球蛋白-肌动蛋白相互作用的三态模型能够在体内或体外预测快速骨骼肌的能量与瞬态和稳态机械特性之间的已知关系,前提是肌球蛋白运动在缩短过程中可以在一个 ATP 水解循环中与两个肌动蛋白位点相互作用。模型的分子细节的实现应该通过利用由长度或叠加在等长收缩上的力的逐步扰动引起的瞬态中存在的动力学和结构约束来实现。
The mechanical performances of the vertebrate skeletal muscle during isometric and isotonic contractions are interfaced with the corresponding energy consumptions to define the coupling between mechanical and biochemical steps in the myosin–actin energy transduction cycle. The analysis is extended to a simplified synthetic nanomachine in which eight HMM molecules purified from fast mammalian skeletal muscle are brought to interact with an actin filament in the presence of 2 mM ATP, to assess the emergent properties of a minimum number of motors working in ensemble without the effects of both the higher hierarchical levels of striated muscle organization and other sarcomeric, regulatory and cytoskeleton proteins. A three-state model of myosin–actin interaction is able to predict the known relationships between energetics and transient and steady-state mechanical properties of fast skeletal muscle either in vivo or in vitro only under the assumption that during shortening a myosin motor can interact with two actin sites during one ATP hydrolysis cycle. Implementation of the molecular details of the model should be achieved by exploiting kinetic and structural constraints present in the transients elicited by stepwise perturbations in length or force superimposed on the isometric contraction.
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