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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.

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.

Pubmed ID: 18838386

Authors

  • Wang YL
  • Faiola F
  • Xu M
  • Pan S
  • Martinez E

Journal

The Journal of biological chemistry

Publication Data

December 5, 2008

Associated Grants

  • Agency: NCI NIH HHS, Id: CA100464

Mesh Terms

  • Acetylesterase
  • Animals
  • Drosophila
  • Genes, Reporter
  • Histone Acetyltransferases
  • Histones
  • Humans
  • Phosphoproteins
  • Protein Folding
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins
  • TATA-Box Binding Protein
  • Transcription Factors
  • Transcription, Genetic
  • Two-Hybrid System Techniques
  • p300-CBP Transcription Factors
  • p38 Mitogen-Activated Protein Kinases