Molodtsov M I, Grishchuk E L, Efremov A K, McIntosh J R, Ataullakhanov F I
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4353-8. doi: 10.1073/pnas.0501142102. Epub 2005 Mar 14.
Chromosome movement during mitosis is powered in part by energy released through the depolymerization of kinetochore microtubules (MTs). Strong but indirect evidence suggests the existence of a specialized coupling between kinetochores and MT plus ends that enables this transduction of chemical energy into mechanical work. Analysis of this phenomenon is important for learning how energy is stored within the MT lattice, how it is transduced, and how efficient the process can be, given coupling devices of different designs. Here we use a recently developed molecular-mechanical model of MTs to examine the mechanism of disassembly dependent force generation. Our approach is based on changes in tubulin dimer conformation that occur during MT disassembly. We find that all of the energy of polymerization-associated GTP hydrolysis can be stored as deformations of the longitudinal bonds between tubulin dimers, and its optimal use does not require the weakening of lateral bonds between dimers. Maximum utilization of this stored energy and, hence, the generation of the strongest possible force, is achieved by a protofilament power-stroke mechanism, so long as the coupling device does not restrict full dissociation of the lateral bonds between tubulin dimers.
有丝分裂过程中的染色体运动部分由动粒微管(MTs)解聚释放的能量驱动。有力但间接的证据表明,动粒与微管正端之间存在一种特殊的耦合,使得这种化学能向机械功的转换成为可能。分析这一现象对于了解能量如何存储在微管晶格中、如何转换以及在不同设计的耦合装置下该过程的效率如何至关重要。在这里,我们使用最近开发的微管分子力学模型来研究依赖于解聚的力产生机制。我们的方法基于微管解聚过程中微管蛋白二聚体构象的变化。我们发现,与聚合相关的GTP水解的所有能量都可以作为微管蛋白二聚体之间纵向键的变形而存储,并且其最佳利用并不需要二聚体之间横向键的减弱。只要耦合装置不限制微管蛋白二聚体之间横向键的完全解离,通过原丝动力冲程机制就能实现这种存储能量的最大利用,从而产生最强的力。