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.
MeSH terms
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Acetyltransferases / chemistry*
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Amino Acid Sequence
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DNA-Binding Proteins / isolation & purification*
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Fungal Proteins
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HeLa Cells
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Histone Acetyltransferases
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Histones / isolation & purification*
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Humans
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Macromolecular Substances
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Mass Spectrometry
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Molecular Sequence Data
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Nuclear Proteins / isolation & purification*
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Protein Kinases
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Saccharomyces cerevisiae Proteins*
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Sequence Analysis
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Sequence Homology, Amino Acid
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Transcription Factors / isolation & purification*
Substances
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DNA-Binding Proteins
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Fungal Proteins
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Histones
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Macromolecular Substances
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NGG1 protein, S cerevisiae
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Nuclear Proteins
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SPT3 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Acetyltransferases
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Histone Acetyltransferases
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Protein Kinases
Associated data
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GENBANK/AF069732
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GENBANK/AF069733
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GENBANK/AF069734
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GENBANK/AF069735
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GENBANK/AF069736