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组蛋白乙酰化在转录因子接近核小体DNA过程中的积极作用。

A positive role for histone acetylation in transcription factor access to nucleosomal DNA.

作者信息

Lee D Y, Hayes J J, Pruss D, Wolffe A P

机构信息

Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.

出版信息

Cell. 1993 Jan 15;72(1):73-84. doi: 10.1016/0092-8674(93)90051-q.

Abstract

Acetylation of the N-terminal tails of the core histones directly facilitates the recognition by TFIIIA of the 5S RNA gene within model chromatin templates. This effect is independent of a reduction in the extent of histone-DNA interactions or a change in DNA helical repeat; it is also independent of whether a histone tetramer or octamer inhibits TFIIIA binding. Removal of the N-terminal tails from the core histones also facilitates the association of TFIIIA with nucleosomal templates. We suggest that the histone tails have a major role in restricting transcription factor access to DNA and that their acetylation releases this restriction by directing dissociation of the tails from DNA and/or inducing a change in DNA configuration on the histone core to allow transcription factor binding. Acetylation of core histones might be expected to exert a major influence on the accessibility of chromatin to regulatory molecules.

摘要

核心组蛋白N端尾部的乙酰化直接促进了TFIIIA对模型染色质模板中5S RNA基因的识别。这种效应与组蛋白-DNA相互作用程度的降低或DNA螺旋重复序列的变化无关;它也与组蛋白四聚体或八聚体是否抑制TFIIIA结合无关。从核心组蛋白上去除N端尾部也促进了TFIIIA与核小体模板的结合。我们认为组蛋白尾部在限制转录因子接近DNA方面起主要作用,并且它们的乙酰化通过引导尾部与DNA解离和/或诱导组蛋白核心上的DNA构象变化以允许转录因子结合来解除这种限制。核心组蛋白的乙酰化可能会对染色质对调节分子的可及性产生重大影响。

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