Shin Jennifer H, Mahadevan L, Waller Guillermina S, Langsetmo Knut, Matsudaira Paul
Department of Mechanical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
J Cell Biol. 2003 Sep 29;162(7):1183-8. doi: 10.1083/jcb.200304006.
During the 5 s of the acrosome reaction of Limulus polyphemus sperm, a 60-microm-long bundle of scruin-decorated actin filaments straightens from a coiled conformation and extends from the cell. To identify the motive force for this movement, we examined the possible sources of chemical and mechanical energy and show that the coil releases approximately 10-13 J of stored mechanical strain energy, whereas chemical energy derived from calcium binding is approximately 10-15 J. These measurements indicate that the coiled actin bundle extends by a spring-based mechanism, which is distinctly different from the better known polymerization or myosin-driven processes, and that calcium initiates but does not power the reaction.
在美洲鲎精子顶体反应的5秒内,一束由丝氨酸蛋白酶修饰的肌动蛋白丝,长度为60微米,从卷曲构象伸直并从细胞中伸出。为了确定这种运动的驱动力,我们研究了化学能和机械能的可能来源,并表明卷曲结构释放出约10 - 13焦耳的储存机械应变能,而钙结合产生的化学能约为10 - 15焦耳。这些测量结果表明,卷曲的肌动蛋白束通过基于弹簧的机制伸展,这与更为人熟知的聚合或肌球蛋白驱动的过程明显不同,并且钙启动但不为该反应提供动力。