Gcn5p is involved in the acetylation of histone H3 in nucleosomes

被引：52

作者：

RuizGarcia, AB ^{[1
]}

Sendra, R ^{[1
]}

Pamblanco, M ^{[1
]}

Tordera, V ^{[1
]}

机构：

[1] UNIV VALENCIA,DEPT BIOQUIM & BIOL MOL,E-46100 BURJASSOT,VALENCIA,SPAIN

来源：

FEBS LETTERS | 1997年 / 403卷 / 02期

关键词：

chromatin; acetylation; histone acetyltransferase; GCN5; nucleosome; Saccharomyces cerevisiae;

D O I：

10.1016/S0014-5793(97)00049-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Enzymatic extracts from a gcn5 mutant and wild-type strains of Saccharomyces cerevisiae were chromatographically fractionated and the histone acetyltransferase activities compared. When free histones were used as substrate, extracts from wild-type cells showed two peaks of activity on histone H3 but extracts from gcn5 mutant cells showed only one. With nucleosomes as substrate, the histone acetyltransferase activities present in extracts from the gcn5 mutant strain were not able to modify H3 whereas wild-type cell extracts acetylated intensely this histone. The activity that acetylated nucleosome-bound H3 behaved as a 170-kDa complex. We suggest that Gcn5p represents a catalytic subunit within a multiprotein complex containing proteins that confer on it the ability to acetylate H3 in nucleosomes. (C) 1997 Federation of European Biochemical Societies.

引用

页码：186 / 190

页数：5

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