Steinmetz M O, Stoffler D, Hoenger A, Bremer A, Aebi U
M. E. Müller Institute for Microscopy, Biozentrum, University of Basel, Switzerland.
J Struct Biol. 1997 Aug;119(3):295-320. doi: 10.1006/jsbi.1997.3873.
Over the past 2 decades our knowledge about actin filaments has evolved from a rigid "pearls on a string" model to that of a complex, highly dynamic protein polymer which can now be analyzed at atomic detail. To achieve this, exploring actin's oligomerization, polymerization, polymorphism, and dynamic behavior has been crucial to understanding in detail how this abundant and ubiquitous protein can fulfill its various functions within living cells. In this review, a correlative view of a number of distinct aspects of actin is presented, and the functional implications of recent structural, biochemical, and mechanical data are critically evaluated. Rational analysis of these various experimental data is achieved using an integrated structural approach which combines intermediate-resolution electron microscopy-based 3-D reconstructions of entire actin filaments with atomic resolution X-ray data of monomeric and polymeric actin.
在过去的20年里,我们对肌动蛋白丝的认识已从僵硬的“串珠”模型发展到如今可以在原子层面进行分析的复杂、高度动态的蛋白质聚合物模型。为实现这一点,探究肌动蛋白的寡聚化、聚合、多态性及动态行为对于详细理解这种丰富且普遍存在的蛋白质如何在活细胞内发挥其各种功能至关重要。在本综述中,我们呈现了肌动蛋白多个不同方面的相关观点,并对近期结构、生化及力学数据的功能意义进行了批判性评估。通过一种综合结构方法对这些各种实验数据进行合理分析,该方法将基于中分辨率电子显微镜的完整肌动蛋白丝三维重建与单体及聚合肌动蛋白的原子分辨率X射线数据相结合。