Journal
MOLECULAR CELL
Volume 9, Issue 3, Pages 553-562Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(02)00478-1
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Nuclear receptors (NRs) regulate transcription in a [ligand-dependent way through two types of coactivator complexes: the p160/CBP histone acetyl transferase (HAT) complex and the DRIP/TRAP/SMCC complex without HAT activity. Here we identified a large human (h) coactivator complex necessary for the estrogen receptor alpha (ERalpha) transactivation. This complex contains the GCN5 HAT, the c-Myc interacting protein TRRAP/PAF400, TAF1130, and other subunits. Similarly to known TFTC (TBP-free TAFII-containing)-type HAT complexes (hTFTC, hPCAF, and hSTAGA), TRRP directly interacted with liganded ERalpha, or other NRs. ERalpha transactivation was enhanced by the purified complex in vitro. Antisense TRRAP RNA inhibited estrogendependent cell growth of breast cancer cells. Thus, the isolated TFTC-type HAT complex acts as a third class of coactivator complex for NR function.
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