Kashiyama T, Ito K, Yamamoto K
Department of Biology, Chiba University, Chiba, Inage-ku, 263-8522, Japan.
J Mol Biol. 2001 Aug 17;311(3):461-6. doi: 10.1006/jmbi.2001.4883.
We succeeded in expressing a chimeric myosin that comprises the motor domain of characean algal myosin, (the fastest known motor protein), and the neck and tail domains of Dictyostelium myosin II. Although the chimeric myosin showed an ATPase activity comparable to that of muscle myosin (15 times higher than that of the wild-type Dictyostelium myosin II), the motile activity of the chimera was only 1.3 times higher than that of the wild-type. However, this is the first chimeric myosin that showed motile activity faster than at least one of the parent myosins. It was suggested, therefore, that the motor domain of Chara myosin has the potential for performing fast sliding movement.
我们成功表达了一种嵌合肌球蛋白,它由轮藻肌球蛋白的马达结构域(已知最快的马达蛋白)以及盘基网柄菌肌球蛋白II的颈部和尾部结构域组成。尽管嵌合肌球蛋白显示出与肌肉肌球蛋白相当的ATP酶活性(比野生型盘基网柄菌肌球蛋白II高15倍),但该嵌合体的运动活性仅比野生型高1.3倍。然而,这是首个运动活性比至少一种亲本肌球蛋白更快的嵌合肌球蛋白。因此,有人提出,轮藻肌球蛋白的马达结构域具有进行快速滑动运动的潜力。