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使用甲醛作为可逆交联剂对核小体中的组蛋白组织进行的研究。

Studies on histone organization in the nucleosome using formaldehyde as a reversible cross-linking agent.

作者信息

Jackson V

出版信息

Cell. 1978 Nov;15(3):945-54. doi: 10.1016/0092-8674(78)90278-7.

Abstract

A new procedure is described which allows selective reversal of formaldehyde cross-linking in both histone-histone and histone-DNA of nuclei isolated from calf thymus. All ten possible dimers of the four non-H1 histones, H3, H2B, H2A and H4, are observed, the major dimers being H3-H3, H3-H2A, H2B-H2A, H2a-H2A and two separate dimers of H2B-H4. Although oligomers of the non-H1 histones are formed by prolonged treatment with this reagent, 50% of the histones continue to remain resistant to cross-linking with each other. For those histones which cross-linking with each other. For those histones which cross-link, the site of cross-linking within the molecules is located in the "core" (trysin-resistant) regionand therfore indicates proximities for these molecules within the nucleosome. The core region also cross-links to DNA, indicating intimate interactions between this region in all the non-H1 histones with DNA.

摘要

本文描述了一种新方法,该方法可选择性地逆转从小牛胸腺分离的细胞核中组蛋白与组蛋白之间以及组蛋白与DNA之间的甲醛交联。观察到四种非H1组蛋白H3、H2B、H2A和H4的所有十种可能的二聚体,主要二聚体为H3-H3、H3-H2A、H2B-H2A、H2a-H2A以及H2B-H4的两种不同二聚体。尽管用该试剂长时间处理会形成非H1组蛋白的寡聚体,但50%的组蛋白彼此之间仍保持抗交联状态。对于那些相互交联的组蛋白,分子内的交联位点位于“核心”(抗胰蛋白酶)区域,因此表明这些分子在核小体内彼此接近。核心区域也与DNA交联,表明所有非H1组蛋白中的该区域与DNA之间存在密切相互作用。

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