Suppr超能文献

多头绒泡菌中组蛋白乙酰化的核内定位及功能活性染色质的结构

Intranuclear localization of histone acetylation in Physarum polycephalum and the structure of functionally active chromatin.

作者信息

Waterborg J H, Matthews H R

出版信息

Cell Biophys. 1983 Dec;5(4):265-79. doi: 10.1007/BF02788625.

Abstract

Based on studies of histone acetylation in vivo in Physarum polycephalum, we present the following hypotheses: (1) Transcription-specific histone acetylation on histones H3 and H4 is a localized process at the nuclear matrix; (2) Histone acetylation in the S phase, which is specific for newly synthesized histones, occurs in an intranuclear nonlocalized process. These hypotheses can explain: (1) the histone specificity of histone acetylation that is dependent on the functional state of the chromatin; (2) the apparent absence of turnover of histone acetylation in the bulk of the chromatin despite a definite low level of steady-state acetylation of all four core histones in bulk chromatin; (3) the pattern of butyrate-induced hyperacetylation observed for active and inactive chromatin.

摘要

基于对多头绒泡菌体内组蛋白乙酰化的研究,我们提出以下假设:(1)组蛋白H3和H4上的转录特异性组蛋白乙酰化是在核基质处的局部过程;(2)S期新合成组蛋白特异性的组蛋白乙酰化发生在核内非局部化过程中。这些假设可以解释:(1)依赖于染色质功能状态的组蛋白乙酰化的组蛋白特异性;(2)尽管整体染色质中所有四种核心组蛋白的稳态乙酰化水平确实较低,但在大部分染色质中组蛋白乙酰化明显缺乏周转;(3)在活性和非活性染色质中观察到的丁酸盐诱导的超乙酰化模式。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验