Myosin binding to actin. Structural analysis using myosin fragments.
Myosin binding to actin. Structural analysis using myosin fragments.
复制标题
肌球蛋白与肌动蛋白结合。
DOI：
10.1016/0022-2836(87)90420-7
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发表时间：
1987
影响因子：
5.6
通讯作者：
Cohen,C
中科院分区：
文献类型：
--
作者：
Castellani,L;ElliottJr,BW;Winkelmann,DA;Vibert,P;Cohen,C
肌动蛋白结合特性的肌球蛋白头20 K（K = 103 Mr）片段已被检查的结构分析。用赖氨酸特异性蛋白酶消化扇贝肌球蛋白合成丝，产生一个新的片段。该片段由杆以及对应于20 K片段的两个“nub”组成，其保留调节轻链和必需轻链。肌球蛋白丝，消化不同的时间长度，混合F-肌动蛋白和可视化的负染色后，通过电子显微镜。当头部被切割，但头部片段仍然相连时，细丝以ATP敏感的方式结合肌动蛋白。然而，主要由含有小块的片段组成的纤维与肌动蛋白的结合非常差。此外，肌动蛋白结合的分离的胰蛋白酶20 K片段从鸡肌球蛋白的电子显微镜表征表明，该片段的结合肌动蛋白可能是非特异性的。这些结果表明，20 K区域和头部的其他肽之间的相互作用是必不可少的肌动蛋白结合。
The actin-binding property of the myosin head 20 K (K = 103Mr) fragment has been examined by a structural assay. A new fragment is produced by digestion of scallop myosin synthetic filaments with a lysine-specific protease. This fragment consists of the rod together with two “nubs” corresponding to the 20 K fragment, which retain both the regulatory and essential light chains. Myosin filaments, digested for different lengths of time, were mixed with F-actin and visualized by electron microscopy after negative staining. When the head is cleaved, but the head fragments remain associated, the filaments bind actin in an ATP-sensitive manner. Filaments made primarily of the nub-containing fragments, however, bind actin very poorly. In addition, electron microscopic characterization of actin-binding by the isolated tryptic 20 K fragment from chicken myosin indicates that binding of this fragment to actin is probably non-specific. These results suggest that interactions between the 20 K region and the other peptides in the head are essential for actin-binding.