Regulation of histone acetylation and transcription by nuclear protein pp32, a subunit of the INHAT complex

被引：123

作者：

Seo, SB ^{[1
]}

Macfarlan, T ^{[1
]}

McNamara, P ^{[1
]}

Hong, R ^{[1
]}

Mukai, Y ^{[1
]}

Heo, S ^{[1
]}

Chakravarti, D ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Pharmacol, Philadelphia, PA 19104 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2002年 / 277卷 / 16期

关键词：

D O I：

10.1074/jbc.M112455200

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：

Histone acetylation by p300/CBP and PCAF coactivators is considered to be a key mechanism of chromatin modification and transcriptional regulation. A multiprotein cellular complex, INHAT (inhibitor of acetyltransferases), containing the Set/TAF-Ibeta oncoprotein and pp32 strongly inhibits the HAT activity of p300/CBP and PCAF by histone masking. Here we report that the INHAT complex and its subunits have overlapping but distinct RAT inhibitory and histone binding characteristics. We provide evidence suggesting that the histone binding and INHAT activity of pp32 can be regulated by its physical association with other INHAT subunits. In vivo colocalization and transfection studies show that pp32 INHAT domains are responsible for histone binding, HAT inhibitory activity, and repression of transcription. We propose that INHAT and its subunits may function by modulating histone acetyltransferases through a histone-masking mechanism and may play important regulatory roles in the establishment and maintenance of the newly proposed "histone code" of chromatin.

引用

页码：14005 / 14010

页数：6

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