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核小体和染色质中的DNA-蛋白质相互作用。通过紫外线诱导交联稳定的染色质的结构研究。

DNA-protein interactions in nucleosomes and in chromatin. Structural studies of chromatin stabilized by ultraviolet-light induced crosslinking.

作者信息

Mandel R, Kolomijtseva G, Brahms J G

出版信息

Eur J Biochem. 1979 May 15;96(2):257-65. doi: 10.1111/j.1432-1033.1979.tb13036.x.

Abstract

Crosslinking induced by ultraviolet light irradiation at 254 nm has been utilized to investigate the structure of chromatin and isolated nucleosomes. The results presented here imply that the four core histones, as well as histone H1, have reactive groups within a bond length of the DNA bases. In nucleosomes depleted of H1, all of the core histones react similarly with the DNA and form crosslinks. In chromatin, the rate of crosslinking of all histones to DNA is essentially similar. Comparison of mononucleosomes, dinucleosomes and whole chromatin shows that the rate of crosslinking increases significantly with increasing number of connected nucleosomes. These differences in the rate of crosslinking are interpreted in terms of interactions between neighbouring nucleosomes on the chromatin fiber, which are absent in an isolated mononucleosome.

摘要

利用254nm紫外线照射诱导的交联作用来研究染色质和分离的核小体的结构。此处呈现的结果表明,四种核心组蛋白以及组蛋白H1在DNA碱基的键长范围内具有反应基团。在缺乏H1的核小体中,所有核心组蛋白与DNA的反应相似并形成交联。在染色质中,所有组蛋白与DNA的交联速率基本相似。单核小体、双核小体和整个染色质的比较表明,交联速率随着相连核小体数量的增加而显著增加。交联速率的这些差异是根据染色质纤维上相邻核小体之间的相互作用来解释的,而在分离的单核小体中不存在这种相互作用。

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