Coordination of a transcriptional switch by HMGI(Y) acetylation

被引：188

作者：

Munshi, N ^{[1
]}

Agalioti, T ^{[1
]}

Lomvardas, S ^{[1
]}

Merika, M ^{[1
]}

Chen, GY ^{[1
]}

Thanos, D ^{[1
]}

机构：

[1] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA

来源：

SCIENCE | 2001年 / 293卷 / 5532期

关键词：

D O I：

10.1126/science.293.5532.1133

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Dynamic control of interferon-beta (IFN-beta) gene expression requires the regulated assembly and disassembly of the enhanceosome, a higher-order nucleoprotein complex formed in response to virus infection. The enhanceosome activates transcription by recruiting the histone acetyltransferase proteins CREB binding protein (CBP) and (p) under bar 300/(C) under bar BP-(a) under bar ssociated (f) under bar actors (PCAF)/GCN5, which, in addition to modifying histones, acetylate HMGI(Y), the architectural component required for enhanceosome assembly. We show that the accurate execution of the IFN-P transcriptional switch depends on the ordered acetylation of the high-mobility group I protein HMGI(Y) by PCAF/GCN5 and CBP, which acetylate HMGI(Y) at distinct lysine residues on endogenous promoters. Whereas acetylation of HMGI(Y) by CBP at lysine-65 destabilizes the enhanceosome, acetylation of HMGI(Y) by PCAF/GCN5 at lysine-71 potentiates transcription by stabilizing the enhanceosome and preventing acetylation by CBP.

引用

页码：1133 / 1136

页数：4

共 10 条

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