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Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2008 Dec 05; Vol. 283 (49), pp. 33808-15. Date of Electronic Publication: 2008 Oct 06. - Publication Year :
- 2008
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Abstract
- Eukaryotic GCN5 acetyltransferases influence diverse biological processes by acetylating histones and non-histone proteins and regulating chromatin and gene-specific transcription as part of multiprotein complexes. In lower eukaryotes and invertebrates, these complexes include the yeast ADA complex that is still incompletely understood; the SAGA (Spt-Ada-Gcn5 acetylase) complexes from yeast to Drosophila that are mostly coactivators; and the ATAC (Ada Two-A containing) complex, only known in Drosophila and still poorly characterized. In contrast, vertebrate organisms, express two paralogous GCN5-like acetyltransferases (GCN5 and PCAF), which have been found so far only in SAGA-type complexes referred to hereafter as the STAGA (SPT3-TAF9-GCN5/PCAF acetylase) complexes. We now report the purification and characterization of vertebrate (human) ATAC-type complexes and identify novel components of STAGA. We show that human ATAC complexes incorporate in addition to GCN5 or PCAF (GCN5/PCAF), other epigenetic coregulators (ADA2-A, ADA3, STAF36, and WDR5), cofactors of chromatin assembly/remodeling and DNA replication machineries (POLE3/CHRAC17 and POLE4), the stress- and TGFbeta-activated protein kinase (TAK1/MAP3K7) and MAP3-kinase regulator (MBIP), additional cofactors of unknown function, and a novel YEATS2-NC2beta histone fold module that interacts with the TATA-binding protein (TBP) and negatively regulates transcription when recruited to a promoter. We further identify the p38 kinase-interacting protein (p38IP/FAM48A) as a novel component of STAGA with distant similarity to yeast Spt20. These results suggest that vertebrate ATAC-type and STAGA-type complexes link specific extracellular signals to modification of chromatin structure and regulation of the basal transcription machinery.
- Subjects :
- Acetylesterase chemistry
Animals
Drosophila
Genes, Reporter
Humans
Phosphoproteins physiology
Protein Folding
Protein Structure, Tertiary
TATA-Box Binding Protein metabolism
Transcription Factors physiology
Transcription, Genetic
Two-Hybrid System Techniques
p38 Mitogen-Activated Protein Kinases metabolism
Acetylesterase physiology
Histone Acetyltransferases chemistry
Histones chemistry
Phosphoproteins metabolism
Saccharomyces cerevisiae Proteins chemistry
TATA-Box Binding Protein chemistry
Transcription Factors metabolism
p300-CBP Transcription Factors chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 283
- Issue :
- 49
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 18838386
- Full Text :
- https://doi.org/10.1074/jbc.M806936200