原胸腺素α在体外与组蛋白H1结合。
Prothymosin alpha binds to histone H1 in vitro.
作者信息
Papamarcaki T, Tsolas O
机构信息
Laboratory of Biological Chemistry, University of Ioannina Medical School, Greece.
出版信息
FEBS Lett. 1994 May 23;345(1):71-5. doi: 10.1016/0014-5793(94)00439-0.
Previous studies have shown that prothymosin alpha (ProT alpha) is a nuclear acidic protein implicated in cell proliferation. To identify proteins that interact with ProT alpha we have used ligand-blotting assays. We report here that purified ProT alpha binds specifically to histone H1 in a dose dependent manner. Polyglutamic acid, an analog of the central acidic domain of ProT alpha, strongly inhibits the above interaction, suggesting that the binding of ProT alpha to histone H1 is mediated through its acidic domain.
先前的研究表明，前胸腺素α（ProTα）是一种与细胞增殖有关的核酸性蛋白。为了鉴定与ProTα相互作用的蛋白质，我们使用了配体印迹分析。我们在此报告，纯化的ProTα以剂量依赖的方式与组蛋白H1特异性结合。聚谷氨酸是ProTα中央酸性结构域的类似物，强烈抑制上述相互作用，这表明ProTα与组蛋白H1的结合是通过其酸性结构域介导的。
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