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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments
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Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments

机译：纤溶蛋白与原肌球蛋白和肌动蛋白丝直接但顺序结合的证据

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Titin is a giant molecule that spans half a sarcomere, establishing several specific bindings with both structural and contractile myofibrillar elements. It has been demonstrated that this giant protein plays a major role in striated muscle cell passive tension and contractile filament alignment. The in vitro interaction of titin with a new partner (tropomyosin) reported here is reinforced by our recent in vitro motility study using reconstituted Ca-regulated thin filaments, myosin and a native 800-kDa titin fragment. In the presence of the tropomyosin–troponin complex, the actin filament movement onto coated S1 is improved by the titin fragment. Here, we found that two purified native titin fragments of 150 and 800 kDa, covering respectively the N1-line and the N2-line/PEVK region in the I-band and known to contain actin-binding sites, directly bind tropomyosin in the absence of actin. We have also shown that binding of the 800-kDa fragment with filamentous actin inhibited the subsequent interaction of tropomyosin with actin, as judged by cosedimentation. However, this was not the case if the complex of actin and tropomyosin was formed before the addition of the 800-kDa fragment. We thus conclude that a sequential arrangement of contacts exists between parts of the titin I-band region, tropomyosin and actin in the thin filament.
机译：Titin是跨过一个肌节的巨大分子，与肌原纤维的结构性和收缩性分子建立了几种特异性结合。已经证明，这种巨大的蛋白质在横纹肌细胞被动张力和收缩性细丝排列中起主要作用。我们最近的体外动力研究使用重组的Ca调节细丝，肌球蛋白和800 kDa天然titin片段，加强了titin与新伴侣（原肌球蛋白）的体外相互作用。在原肌球蛋白-肌钙蛋白复合物的存在下，肌动蛋白丝移动到包被的S1上的肌动蛋白片段将得到改善。在这里，我们发现150和800 kDa的两个纯化的天然山雀蛋白片段分别覆盖I波段中的N1线和N2线/ PEVK区，并且已知包含肌动蛋白结合位点，在不存在的情况下直接结合原肌球蛋白肌动蛋白。我们还显示，通过共沉淀可以判断，800 kDa片段与丝状肌动蛋白的结合抑制了原肌球蛋白与肌动蛋白的后续相互作用。但是，如果在添加800 kDa片段之前形成了肌动蛋白和原肌球蛋白的复合物，则情况并非如此。因此，我们得出的结论是，细丝中的titin I带区域，原肌球蛋白和肌动蛋白之间存在接触的顺序排列。

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