Leffak I M, Li H J
Biochim Biophys Acta. 1981 Nov 27;656(1):86-92. doi: 10.1016/0005-2787(81)90030-7.
The nucleotide sequence selectivity of histone binding has been measured by thermal denaturation of reconstituted nucleoproteins. When DNAs of different average base compositions competed for the binding of purified histone fractions during in vitro reconstitutions in the presence of salt and urea, a decreasing (A + T)-binding preference was observed following the order H1 greater than H2B greater than H5 greater than H2A greater than [H2A + H2B] greater than [H2A + H2B + H3 + H4], [H1 + (H2A + H2B + H3 + H4)2]. Nucleoprotein complexes formed under conditions shown to yield more physiologically comparable nucleosome structures revealed a minimal (A + T)-binding preference. These results suggest that homotypic and heterotypic histone interactions decreased the nucleotide sequence selectivity of nucleosome binding.
通过重构核蛋白的热变性测定了组蛋白结合的核苷酸序列选择性。当不同平均碱基组成的DNA在盐和尿素存在下进行体外重构过程中竞争纯化组蛋白组分的结合时，观察到结合偏好（A + T）递减，顺序为H1＞H2B＞H5＞H2A＞[H2A + H2B]＞[H2A + H2B + H3 + H4]，[H1 +（H2A + H2B + H3 + H4）2]。在显示产生更具生理可比性的核小体结构的条件下形成的核蛋白复合物显示出最小的（A + T）结合偏好。这些结果表明，同型和异型组蛋白相互作用降低了核小体结合的核苷酸序列选择性。
