Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60

被引：204

作者：

Yamamoto, T ^{[1
]}

Horikoshi, M ^{[1
]}

机构：

[1] Univ Tokyo, Inst Mol & Cellular Biol, Dept Cellular Biol, Dev Biol Lab,Bunkyo Ku, Tokyo 113, Japan

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1997年 / 272卷 / 49期

关键词：

D O I：

10.1074/jbc.272.49.30595

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：

Tip60, originally isolated as an HIV-1-Tat interactive protein, contains an evolutionarily conserved domain with yeast silencing factors, We demonstrate here direct biochemical evidence that this domain of Tip60 has histone acetyltransferase activity, The purified recombinant effectively acetylates H2A, H3, and H4 but not H2B of core histone mixtures, This substrate specificity has not been observed among histone acetyltransferases analyzed to date. These results indicate that Tip60 is a histone acetyltransferase with a novel property, suggesting that Tip60 and its related factors may introduce a distinct alteration on chromatin.

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页码：30595 / 30598

页数：4

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