Mapping the binding domain of a myosin II binding protein.
Mapping the binding domain of a myosin II binding protein.
复制标题
绘制肌球蛋白 II 结合蛋白的结合域图。
DOI：
10.1021/bi00106a019
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发表时间：
1991
期刊：
影响因子：
2.9
通讯作者：
Burgess,DR
中科院分区：
文献类型：
--
作者：
Walker,G;Yabkowitz,R;Burgess,DR
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260 Received January 3, 1991; Revised Manuscript Received June 3, 1991 abstract: The way in which actin and myosin II become localized to the contractile ring of dividing cells resulting in cleavage furrow formation and cytokinesis is unknown. While much is known about actin binding proteins and actin localization, little is known about myosin localization. A 53-kDa (53K) polypeptide present in the sea urchin egg binds to myosin II in a nucleotide-dependent manner and mediates its solubility in vitro [Yabkowitz, R., & Burgess, DR (1987) J. Cell Biol. 105, 927-936]. The binding site of 53K on the myosin molecule was examined in an effort tounderstand the mechanism of 53K-induced myosin solubility and its potentialfunction in myosin regulation. Blot overlayand chemical cross-linking techniques utilizing myosin proteolytic fragments indicatethat 53K binds to fragments proximal to the head-rod junction of myosin. Fragments distal to the head-rod junction do not bind 53K. In addition, the binding of 53K to myosin largely inhibits protease digestion that produces the head and rod fragments. The binding of 53K to the head-rod domain of myosin may be critical in regulation of myosin conformation, localization, assembly, and ATPase activity. e actin-based cytoskeleton of the sea urchin egg cortex plays a vital role in cytokinesis. After fertilization, changes in the cytoskeleton are induced which mediate contractile ring formation and subsequent contraction. Actin and myosin II, the chemomechanical transducer, become concentrated to the
