Histone-like TAFs within the PCAF histone acetylase complex

被引：458

作者：

Ogryzko, VV

Kotani, T

Zhang, XL

Schiltz, RL

Howard, T

Yang, XJ

Howard, BH

Qin, J

Nakatani, Y ^{[1
]}

机构：

[1] NICHHD, Lab Mol Growth Regulat, NIH, Bethesda, MD 20892 USA

[2] NHLBI, Biophys Chem Lab, NIH, Bethesda, MD 20892 USA

来源：

CELL | 1998年 / 94卷 / 01期

关键词：

D O I：

10.1016/S0092-8674(00)81219-2

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：

PCAF histone acetylase plays a role in regulation of transcription, cell cycle progression, and differentiation. Here, we show that PCAF is found in a complex consisting of more than 20 distinct polypeptides. Strikingly, some polypeptides are identical to TBP-associated factors (TAFs), which are subunits of TFIID. Like TFIID, histone fold-containing factors are present within the PCAF complex. The histone H3- and H2B-like subunits within the PCAF complex are identical to those within TFIID, namely, hTAF(II)31 and hTAF(II)20/15, respectively. The PCAF complex has a novel histone H4-like subunit with similarity to hTAF(II)80 that interacts with the histone H3-like domain of hTAF(II)31. Moreover, the PCAF complex has a novel subunit with WD40 repeats having a similarity to hTAF(II)100.

引用

收藏

页码：35 / 44

页数：10

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