Collins C A, Vallee R B
Proc Natl Acad Sci U S A. 1986 Jul;83(13):4799-803. doi: 10.1073/pnas.83.13.4799.
We report an ATPase activity, present in sea urchin egg cytosol, that is activated by microtubules. The activity sediments at 10 S in sucrose gradients and is clearly distinct from activities at 12 S and 20 S due to cytoplasmic dynein. Potent activation of the ATPase is observed when endogenous egg tubulin is induced to assemble with taxol or when exogenous taxol-stabilized pure brain tubulin microtubules or flagellar outer-doublet microtubules are added. No activation by tubulin subunits or taxol alone is detectable. In contrast to flagellar or cytoplasmic dynein, the microtubule-activated enzyme is unaffected by vanadate or by nonionic detergents and hydrolyzes GTP in addition to ATP. In contrast to kinesin, it cosediments with microtubules in the presence or absence of ATP. The microtubule-activated enzyme may have a role in microtubule-based motility.
我们报道了一种存在于海胆卵细胞质溶胶中的ATP酶活性,该活性可被微管激活。该活性在蔗糖梯度中沉降系数为10S,与由于细胞质动力蛋白导致的12S和20S处的活性明显不同。当内源性卵微管蛋白被紫杉醇诱导组装时,或者当添加外源性紫杉醇稳定的纯脑微管蛋白微管或鞭毛外双联微管时,可观察到ATP酶的强力激活。单独的微管蛋白亚基或紫杉醇均未检测到激活作用。与鞭毛或细胞质动力蛋白不同,微管激活的酶不受钒酸盐或非离子去污剂的影响,除了ATP外还能水解GTP。与驱动蛋白不同,无论有无ATP,它都与微管共沉降。微管激活的酶可能在基于微管的运动中起作用。