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嗜热四膜虫大核和小核中组蛋白乙酰化的调控

Regulation of histone acetylation in Tetrahymena macro- and micronuclei.

作者信息

Vavra K J, Allis C D, Gorovsky M A

出版信息

J Biol Chem. 1982 Mar 10;257(5):2591-8.

PMID:7061439
Abstract

Histone acetylation in Tetrahymena macro- and micronuclei has been studied utilizing a combination of electrophoretic and autoradiographic techniques. Histones H2A, H2B, H3, and H4 are acetylated to varying extents in the transcriptionally active macronucleus. There are few, if any, acetylated subspecies of these histones in the transcriptionally inert micronucleus, and micronuclei incorporate little radioactive acetate, either in vivo or in isolated nuclei. Butyrate is shown to inhibit histone deacetylation in Tetrahymena, both in vivo and in isolated nuclei. Incorporation of acetate into micronuclei is unaffected by high concentrations of this inhibitor, indicating that the extremely low levels of histone acetylation observed in micronuclei are not due to rapid deacylation but probably result from the absence of histone acetylation. We also present evidence that macronuclear core histones are composed of at least two classes of molecules distinguishable on the basis of their acetate turnover rates and that individual histone species differ in the distribution of their populations between these classes.

摘要

利用电泳和放射自显影技术相结合的方法,对四膜虫大核和小核中的组蛋白乙酰化进行了研究。在转录活跃的大核中,组蛋白H2A、H2B、H3和H4在不同程度上被乙酰化。在转录惰性的小核中,这些组蛋白几乎没有(如果有的话)乙酰化亚类,并且小核在体内或分离的细胞核中几乎不掺入放射性乙酸盐。已表明丁酸盐在体内和分离的细胞核中均能抑制四膜虫中的组蛋白去乙酰化。高浓度的这种抑制剂不会影响乙酸盐掺入小核,这表明在小核中观察到的极低水平的组蛋白乙酰化不是由于快速脱酰基作用,而是可能由于缺乏组蛋白乙酰化。我们还提供了证据表明,大核核心组蛋白由至少两类基于其乙酸盐周转率可区分的分子组成,并且单个组蛋白种类在这些类别之间的群体分布有所不同。

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