Binding of a native titin fragment to actin is regulated by PIP2
Binding of a native titin fragment to actin is regulated by PIP2
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DOI：
10.1016/s0014-5793(98)00572-9
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发表时间：
1998-06-05
期刊：
影响因子：
3.5
通讯作者：
Benyamin, Y
中科院分区：
文献类型：
--
作者：
Astier, C;Raynaud, F;Benyamin, Y
肌凝蛋白是横纹肌中从z线延伸到m线的巨大蛋白质。我们在此报告了在V8蛋白酶处理肌原纤维后获得的150 kda的titin片段的纯化，该多肽位于n1线水平，位于已知与肌动蛋白相关的titin部分中，通过固相或液相结合试验和共沉淀法，我们清楚地证明了天然titin片段与F-actin的直接，可饱和和相对高亲和力结合。150 kda的titin片段也被证明可以加速肌动蛋白聚合。此外，肌动蛋白-肌动蛋白相互作用被磷酸肌苷抑制。(C) 1998年欧洲生化学会联合会。
Titin is a giant protein which extends from Z-line to M-line in striated muscles. We report here the purification of a 150-kDa titin fragment, obtained after V8 protease treatment of myofibrils, This polypeptide was located at the N1-line level, in a titin part known to exhibit stiff properties correlated to an association with actin, By solid or liquid phase binding assays and cosedimentation, we have clearly demonstrated a direct, saturable and relative high affinity binding of the native titin fragment to F-actin, The 150-kDa titin fragment was also shown to accelerate actin polymerization. Furthermore, the actin-titin interaction was found to be inhibited by phosphoinositides. (C) 1998 Federation of European Biochemical Societies.