Eyer J, White D, Gagnon C
Urology Research Laboratory, Royal Victoria Hospital, Montreal, Quebec, Canada.
Biochem Biophys Res Commun. 1987 Oct 14;148(1):218-24. doi: 10.1016/0006-291x(87)91098-9.
Crude dynein extracted from bull sperm flagella polymerized pure phosphocellulose tubulin isolated from brain tissues into microtubules. This effect was predominantly due to the 19S dynein particle in the extract. ATP stimulated up to five fold the polymerization of brain tubulin by bull sperm dynein. Hydrolysis of ATP was not required since vanadate at a concentration sufficient to block dynein ATPase activity did not interfere with ATP stimulation and because the non hydrolyzable ATP analogue adenylyl (beta-gamma-methylene) diphosphate (AMPPCP) had effects similar to those of ATP. These results suggest that, in addition to hydrolyzing ATP to generate the driving force necessary for microtubule sliding within the axoneme, dynein may also interact with ATP to polymerize tubulin into microtubules.
从公牛精子鞭毛中提取的粗动力蛋白能将从脑组织中分离出的纯磷酸纤维素微管蛋白聚合成微管。这种效应主要归因于提取物中的19S动力蛋白颗粒。ATP能刺激公牛精子动力蛋白使脑微管蛋白的聚合作用增强至五倍。由于浓度足以阻断动力蛋白ATP酶活性的钒酸盐并不干扰ATP的刺激作用,并且因为不可水解的ATP类似物腺苷酰(β-γ-亚甲基)二磷酸(AMPPCP)具有与ATP相似的作用,所以不需要ATP水解。这些结果表明,动力蛋白除了水解ATP以产生轴丝内微管滑动所需的驱动力外,还可能与ATP相互作用,将微管蛋白聚合成微管。