The nuclear Hat1p/Hat2p complex: A molecular link between type B histone acetyltransferases and chromatin assembly

被引：116

作者：

Ai, X ^{[1
]}

Parthun, MR ^{[1
]}

机构：

[1] Ohio State Univ, Dept Mol & Cellular Biochem, Columbus, OH 43210 USA

来源：

MOLECULAR CELL | 2004年 / 14卷 / 02期

关键词：

D O I：

10.1016/S1097-2765(04)00184-4

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：

The yeast Hat1p/Hat2p type B histone acetyltransferase complex is localized to both the cytoplasm and nucleus. We isolate the nuclear form of the Hat1p/ Hat2p complex and find that it copurifies with the product of the uncharacterized open reading frame YLL022C (named Hif1p). The functional significance of the association of Hif1p with the Hat1p/Hat2p complex is confirmed by the observation that hif1Delta and hat1Delta strains display similar defects in telomeric silencing and DNA double-strand break repair. Hif1p is a histone chaperone that selectively interacts with histones H3 and H4. Hif1p is also a chromatin assembly factor, promoting the deposition of histones in the presence of a yeast cytosolic extract. In vivo, the nuclear Hat1p/ Hat2p/Hif1p complex is bound to acetylated histone H4, as well as histone H3. The association of Hif1p with acetylated H4 requires Hat1p and Hat2p providing a link between type B histone acetyltransferases and chromatin assembly.

引用

页码：195 / 205

页数：11

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