van Oudenaarden A, Theriot J A
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Nat Cell Biol. 1999 Dec;1(8):493-9. doi: 10.1038/70281.
Polymerizing networks of actin filaments are capable of exerting significant mechanical forces, used by eukaryotic cells and their prokaryotic pathogens to change shape or to move. Here we show that small beads coated uniformly with a protein that catalyses actin polymerization are initially surrounded by symmetrical clouds of actin filaments. This symmetry is broken spontaneously, after which the beads undergo directional motion. We have developed a stochastic theory, in which each actin filament is modelled as an elastic brownian ratchet, that quantitatively accounts for the observed emergent symmetry-breaking behaviour. Symmetry-breaking can only occur for polymers that have a significant subunit off-rate, such as the biopolymers actin and tubulin.
肌动蛋白丝的聚合网络能够施加显著的机械力,真核细胞及其原核病原体利用这些力来改变形状或移动。我们在此表明,均匀包被有催化肌动蛋白聚合的蛋白质的小珠子,最初被肌动蛋白丝的对称云状物所包围。这种对称性会自发打破,之后珠子会发生定向运动。我们已经发展出一种随机理论,其中每条肌动蛋白丝被建模为一个弹性布朗棘轮,该理论定量地解释了所观察到的突发对称性破缺行为。对称性破缺仅能发生在具有显著亚基解离速率的聚合物中,比如生物聚合物肌动蛋白和微管蛋白。