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Human STAGA Complex Is a Chromatin-Acetylating Transcription Coactivator That Interacts with Pre-mRNA Splicing and DNA Damage-Binding Factors In Vivo
The results suggest cellular roles of STAGA in chromatin modification, transcription, and transcription-coupled processes through direct physical interactions with sequence-specific transcription activators and with components of the splicing and DNA repair machineries.
Cloning of an Inr‐ and E‐box‐binding protein, TFII‐I, that interacts physically and functionally with USF1
It is demonstrated that ectopic TFII‐I and USF1 can act synergistically, and in some cases independently, to activate transcription in vivo through both Inr and the E‐box elements of the adenovirus major late promoter.
Human ATAC Is a GCN5/PCAF-containing Acetylase Complex with a Novel NC2-like Histone Fold Module That Interacts with the TATA-binding Protein*
The 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.
c-Myc Transformation Domain Recruits the Human STAGA Complex and Requires TRRAP and GCN5 Acetylase Activity for Transcription Activation*
It is demonstrated that GCN5 and TRRAP cooperate to enhance transcription activation by the N-terminal activation domain of Myc in vivo and that this synergy requires both the SPT3/GCN5 interaction domain of TRR AP and the HAT activity of GCN 5.
Multi-protein complexes in eukaryotic gene transcription
  • E. Martinez
  • Biology
    Plant Molecular Biology
  • 1 December 2002
Genetic and biochemical studies have recently identified a variety of transcription cofactors/co-regulators that interact with sequence-specific regulators and/or various components of the general/basal transcription machinery and are essential for regulated transcription.
Cooperative binding of estrogen receptor to imperfect estrogen‐responsive DNA elements correlates with their synergistic hormone‐dependent enhancer activity.
It is suggested that the observed synergistic estrogen‐dependent transcription activation conferred by the pair of hormone‐responsive DNA elements of the vit B1 ERU is the result of cooperative binding of two estrogen receptor dimers to these two adjacent imperfect EREs.
Dual Regulation of c-Myc by p300 via Acetylation-Dependent Control of Myc Protein Turnover and Coactivation of Myc-Induced Transcription
P300 functions as a coactivator that is recruited by Myc to the promoter of the human telomerase reverse transcriptase gene, and p300/CBP stimulates Myc TAD-dependent transcription in a HAT domain-dependent manner.
Specific Interactions and Potential Functions of Human TAFII100*
A role for hTAFII100 in stabilizing interactions of TAFs, especially the histone-like TAF's, in TFIID is suggested, suggesting a possible core promoter-specific function for the subunit.
The estrogen‐responsive element as an inducible enhancer: DNA sequence requirements and conversion to a glucocorticoid‐responsive element.
The estrogen‐responsive element (ERE) present in the 5′‐flanking region of the Xenopus laevis vitellogenin (vit) gene B1 has been characterized by transient expression analysis of chimeric vit‐tk‐CAT