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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Acetylated nucleosome assembly on telomeric DNAs
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Acetylated nucleosome assembly on telomeric DNAs

机译：端粒DNA上的乙酰化核小体组装

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摘要

The role of histone N-terminal domains on the thermodynamic stability of nucleosomes assembled on several different telomeric DNAs as well as on 'average' sequence DNA and on strong nucleosome positioning sequences, has been studied by competitive reconstitution. We find that histone tails hyperacetylation favors nucleosome formation, in a similar extent for all the examined sequences. On the contrary, removal of histone terminal domains by selective trypsinization causes a decrease of nucleosome stability which is smaller for telomeres compared to the other sequences examined, suggesting that telomeric sequences have only minor interactions with histone tails. Micrococcal nuclease kinetics shows enhanced accessibility of acetylated nucleosomes formed both on telomeric and 'average' sequence DNAs. These results suggest a more complex role for histone acetylation than the decrease of electrostatic interactions between DNA and histones. (C) 2003 Elsevier Science B.V. All rights reserved. [References: 45]
机译：已通过竞争性重建研究了组蛋白N末端结构域对组装在几种不同端粒DNA以及“平均”序列DNA和强核小体定位序列上的核小体的热力学稳定性的作用。我们发现，组蛋白尾巴的超乙酰化有利于核小体的形成，在所有检查的序列中都相似。相反，通过选择性胰蛋白酶消化去除组蛋白末端结构域会导致核小体稳定性的降低，与其他检测的序列相比，端粒的核小体稳定性要小，这表明端粒序列与组蛋白尾巴之间只有很小的相互作用。微球菌核酸酶动力学显示在端粒和“平均”序列DNA上形成的乙酰化核小体的可及性增强。这些结果表明，组蛋白乙酰化的作用比降低DNA和组蛋白之间静电相互作用的作用更为复杂。 （C）2003 Elsevier Science B.V.保留所有权利。 [参考：45]

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