BRAIN MYOSIN-V IS A 2-HEADED UNCONVENTIONAL MYOSIN WITH MOTOR-ACTIVITY

BRAIN MYOSIN-V IS A 2-HEADED UNCONVENTIONAL MYOSIN WITH MOTOR-ACTIVITY
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DOI:
10.1016/s0092-8674(05)80080-7
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发表时间:
1993-10-08
期刊:
影响因子:
64.5
通讯作者:
MOOSEKER, MS
MOOSEKER, MS
中科院分区:
生物学1区
文献类型:
--
作者:
CHENEY, RE;OSHEA, MK;MOOSEKER, MS

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鸡肌球蛋白-V是最近认识到的一类肌球蛋白的成员,不同于肌球蛋白-I和肌球蛋白-II。我们在这里报告的纯化,电子显微镜可视化,和电机性能的蛋白质这一类。肌球蛋白-V分子由两个头部连接到一个约30 nm的茎,在一个功能未知的球状区域结束。肌球蛋白-V结合并修饰F-肌动蛋白,具有肌动蛋白激活的镁-ATP酶活性,并且是能够以高达400 nm/s的速率移动肌动蛋白丝的有倒钩末端定向马达。肌球蛋白-V不形成细丝。每个肌球蛋白-V重链与大约四个钙调蛋白轻链以及两个丰度较低的23和17 kd蛋白质相关。
Chicken myosin-V is a member of a recently recognized class of myosins distinct from both the myosins-I and the myosins-II. We report here the purification, electron microscopic visualization, and motor properties of a protein of this class. Myosin-V molecules consist of two heads attached to an approximately 30 nm stalk that ends in a globular region of unknown function. Myosin-V binds to and decorates F-actin, has actin-activated magnesium-ATPase activity, and is a barbed-end-directed motor capable of moving actin filaments at rates of up to 400 nm/s. Myosin-V does not form filaments. Each myosin-V heavy chain is associated with approximately four calmodulin light chains as well as two less abundant proteins of 23 and 17 kd.