Coupling of actin hydrolysis and polymerization: Reduced description with two nucleotide states
Coupling of actin hydrolysis and polymerization: Reduced description with two nucleotide states
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肌动蛋白水解和聚合的耦合：用两种核苷酸状态简化描述
DOI：
10.1209/0295-5075/89/38010
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
J. Kierfeld
中科院分区：
文献类型：
--
作者：
Xin Li;R. Lipowsky;J. Kierfeld
肌动蛋白丝的聚合与三磷酸腺苷（ATP）的水解相结合，其中包括ATP的裂解和无机磷酸盐的释放。我们用一种具有协同解理机制的简化双态模型来描述水解，其中解理速率取决于丝中相邻肌动蛋白原聚体的状态。我们获得了实验可获得的稳态量的理论预测，如atp -肌动蛋白帽的大小，atp -肌动蛋白岛的大小分布，以及协同裂解机制的裂解通量。
The polymerization of actin filaments is coupled to the hydrolysis of adenosine triphosphate (ATP), which involves both the cleavage of ATP and the release of inorganic phosphate. We describe hydrolysis by a reduced two-state model with a cooperative cleavage mechanism, where the cleavage rate depends on the state of the neighboring actin protomer in a filament. We obtain theoretical predictions of experimentally accessible steady-state quantities such as the size of the ATP-actin cap, the size distribution of ATP-actin islands, and the cleavage flux for cooperative cleavage mechanisms.