A functional recombinant myosin II lacking a regulatory light chain-binding site.
A functional recombinant myosin II lacking a regulatory light chain-binding site.
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缺乏调节性轻链结合位点的功能性重组肌球蛋白 II。
DOI：
10.1126/science.8266074
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Spudich,JA
中科院分区：
文献类型：
--
作者：
Uyeda,TQ;Spudich,JA
肌球蛋白II是一种由两条重链、两条基本轻链和两条调节轻链(RLC)组成的六角体。Dictyosteliummyosin II在体外通过RLC的磷酸化来调节。野生型肌球蛋白II重链被缺乏RLC结合位点的重组形式取代的细胞进行胞质分裂和几乎正常的发育，这是已知依赖于功能肌球蛋白II的过程。对纯化的重组蛋白的表征表明，RLC和重链上的RLC结合部位的复合体对腺苷三磷酸酶活性具有抑制作用，对肌球蛋白沿肌动蛋白的运动具有结构性作用。
Myosin II, which converts the energy of adenosine triphosphate hydrolysis into the movement of actin filaments, is a hexamer of two heavy chains, two essential light chains, and two regulatory light chains (RLCs).Dictyosteliummyosin II is known to be regulated in vitro by phosphorylation of the RLC. Cells in which the wild-type myosin II heavy chain was replaced with a recombinant form that lacks the binding site for RLC carried out cytokinesis and almost normal development, processes known to be dependent on functional myosin II. Characterization of the purified recombinant protein suggests that a complex of RLC and the RLC binding site of the heavy chain plays an inhibitory role for adenosine triphosphatase activity and a structural role for the movement of myosin along actin.