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鉴定酵母沉默交配位点抑制所需的组蛋白H4 N端非碱性结构域。

Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci.

作者信息

Johnson L M, Fisher-Adams G, Grunstein M

机构信息

Molecular Biology Institute, University of California, Los Angeles 90024.

出版信息

EMBO J. 1992 Jun;11(6):2201-9. doi: 10.1002/j.1460-2075.1992.tb05279.x.

Abstract

We have shown previously that a stretch of four charged residues (16-19) at the histone H4 N-terminus is involved in repression of the yeast silent mating loci. One of these residues, Lys16, is a site for acetylation, which may prevent repression of the silent mating loci. In this paper we ask whether other sequences in histone H4, possibly in conjunction with H3 residues, are required for repression. We find that even in combination, the other seven acetylatable lysines in H3 and H4 do not function in repression. In contrast, we have found that an adjacent relatively uncharged domain (residues 21-29) is required for repression and that single amino acid insertions and deletions in this region are extremely detrimental. We propose that the basic and non-basic domains together form a DNA (or protein) induced amphipathic alpha-helix required in the formation of a repressive chromatin structure.

摘要

我们之前已经表明,组蛋白H4 N端的一段四个带电荷的残基(16 - 19)参与了酵母沉默交配位点的抑制。其中一个残基,赖氨酸16,是乙酰化位点,这可能会阻止沉默交配位点的抑制。在本文中,我们探讨组蛋白H4中的其他序列,可能与H3残基一起,是否是抑制所必需的。我们发现,即使结合起来,H3和H4中的其他七个可乙酰化赖氨酸在抑制中也不起作用。相反,我们发现一个相邻的相对不带电荷的结构域(残基21 - 29)是抑制所必需的,并且该区域中的单个氨基酸插入和缺失极其有害。我们提出,碱性和非碱性结构域共同形成一个DNA(或蛋白质)诱导的两亲性α-螺旋,这是形成抑制性染色质结构所必需的。

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