驱动蛋白的货物激活ATP酶活性。
Cargo-activated ATPase activity of kinesin.
作者信息
Jiang M Y, Sheetz M P
机构信息
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
出版信息
Biophys J. 1995 Apr;68(4 Suppl):283S-284S; discussion 285S.
Abstract
We have measured the ATPase activity of squid optic lobe kinesin bound to polystyrene beads in the presence of microtubules. We find that there is a substantial increase (> 10-fold) in the microtubule-activated ATPase activity for bead-bound kinesin over free kinesin. We tentatively attribute such cargo-activated ATPase activity to the presence of a self-inhibited form of kinesin in solution, which becomes activated when bound to a bead in the presence of alpha-casein. Further experiments are underway to unravel this phenomenon and, in addition, to associate the traveling distance of beads with the observed ATPase rate to determine the average number of ATP consumed per kinesin-bead per micron of travel along microtubule.
摘要
我们测量了在微管存在的情况下，与聚苯乙烯珠结合的鱿鱼视叶驱动蛋白的ATP酶活性。我们发现，与游离驱动蛋白相比，珠结合的驱动蛋白的微管激活ATP酶活性有显著增加（>10倍）。我们初步将这种货物激活的ATP酶活性归因于溶液中存在一种自我抑制形式的驱动蛋白，当在α-酪蛋白存在的情况下与珠子结合时，它会被激活。进一步的实验正在进行中，以揭示这一现象，此外，将珠子的移动距离与观察到的ATP酶速率联系起来，以确定每微米沿微管移动的驱动蛋白-珠子消耗的ATP平均数量。
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