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- W2013890168 abstract "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." @default.
- W2013890168 created "2016-06-24" @default.
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- W2013890168 date "1998-07-01" @default.
- W2013890168 modified "2023-10-18" @default.
- W2013890168 title "Histone-like TAFs within the PCAF Histone Acetylase Complex" @default.
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- W2013890168 doi "https://doi.org/10.1016/s0092-8674(00)81219-2" @default.
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