微管蛋白构象变化的统一假说
A Unifying Hypothesis for the Conformational Change of Tubulin
摘要：
微管动力学不稳定性是由与微管蛋白二聚体的β-单体结合的GTP水解引起的。由水解引起的构象变化是未知的，但微管分解成GDP结合的微管蛋白的原丝，其弯曲远离微管轴。本文提出了一个合理的，统一的解释微管的不同结构和动力学特征的微管蛋白分子的一部分到微管内部展开。这是第一个具体的结构假说的水解诱导的微管蛋白的构象变化，同时解释了削弱的横向债券，弯曲的纵向债券，在原丝超扭曲与GTP水解，GDP微管蛋白双环的结构特征，在较高的温度下更快的拆卸和较慢的拆卸甘油和氧化氘的存在下的变化。这一假设需要进一步的理论研究和直接的实验检验。
英文摘要：
Microtubule dynamic instability arises from the hydrolysis of GTP bound to the beta-monomer of the tubulin dimer. The conformational change induced by hydrolysis is unknown, but microtubules disassemble into protofilaments of GDP-bound tubulin that curve away from the microtubule axis. This paper presents the unfolding of a portion of the tubulin molecule into the microtubule interior as a plausible, unifying explanation for diverse structural and kinetic features of microtubules. This is the first specific structural hypothesis for the hydrolysis induced conformational change of tubulin that simultaneously explains weakening of lateral bonds, bending about longitudinal bonds, changes in protofilament supertwist associated with GTP hydrolysis, structural features of GDP-tubulin double rings, faster disassembly at higher temperatures and slower disassembly in the presence of glycerol and deuterium oxide. The hypothesis suggests further theoretical investigations and direct experimental tests.
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