Interactions of elongation factor 2 with the cytoskeleton and interference with DNase I binding to actin
Interactions of elongation factor 2 with the cytoskeleton and interference with DNase I binding to actin
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DOI：
10.1046/j.1432-1327.1998.2560142.x
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发表时间：
1998-08-01
期刊：
影响因子：
--
通讯作者：
Bermek, E
中科院分区：
文献类型：
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作者：
Bektas, M;Nurten, R;Bermek, E
采用粘度法、凝胶过滤法和电镜技术研究了延伸因子2（EF-2）与G-肌动蛋白和F-肌动蛋白在体外的相互作用。在解聚条件下，在0.5：1（EF-2/F-肌动蛋白亚基）的摩尔比下，F-肌动蛋白被EF-2稳定，并且细丝解聚比仅含有F-肌动蛋白的对照溶液慢约三倍。当EF-2在DNA酶I存在下包含在溶液中时，细丝稳定性也得到改善。电子显微照片和粘度测量表明，EF-2可以支持2或3个长丝宽度的小束。已经确定EF-2在体外与G-肌动蛋白相互作用，并且当其以1：1的比例存在时降低G-肌动蛋白对DNA酶I活性的抑制。结果进行了讨论的背景下可能的功能意义的相互作用。
Interactions of elongation factor 2 (EF-2) with G-actin and F-actin in vitro were investigated using viscosimetry, gel filtration and electron microscopy. Under depolymerization conditions, at a molar ratio of 0.5:1 (EF-2/F-actin subunit), F-actin is stabilised by EF-2 and filaments depolymerize about three times slower than control solutions containing only F-actin. Filament stability is improved also when EF-2 is included in the solution in the presence of DNase I. Electron micrographs and viscosity measurements indicate that EF-2 may support small bundles with a width of 2 or 3 filaments. It was established that EF-2 interacts with G-actin in vitro, and reduces G-actin inhibition of DNase I activity when it is present at a ratio of 1:1. Results are discussed in the context of possible functional significance of the interactions.