Histone-like TAFs within the PCAF histone acetylase complex.
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.
Mesh Terms:
Acetyltransferases, Amino Acid Sequence, DNA-Binding Proteins, Fungal Proteins, Hela Cells, Histone Acetyltransferases, Histones, Humans, Macromolecular Substances, Mass Spectrometry, Molecular Sequence Data, Nuclear Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins, Sequence Analysis, Sequence Homology, Amino Acid, Transcription Factors
Acetyltransferases, Amino Acid Sequence, DNA-Binding Proteins, Fungal Proteins, Hela Cells, Histone Acetyltransferases, Histones, Humans, Macromolecular Substances, Mass Spectrometry, Molecular Sequence Data, Nuclear Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins, Sequence Analysis, Sequence Homology, Amino Acid, Transcription Factors
Cell
Date: Jul. 10, 1998
PubMed ID: 9674425
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