Weinzierl, R.O.J., Ruppert, S., Dynlacht, B.D., Tanese, N., Tjian, R. (1993). Cloning and expression of Drosophila TAF_II60 and human TAF_II70 reveal conserved interactions with other subunits of TFIId.  EMBO J. 12(13): 5303--5309.

FBrf0065607

Research paper

Regulation of transcription initiation by RNA polymerase II requires TFIID, a multisubunit complex composed of the TATA binding protein (TBP) and at least seven tightly associated factors (TAFs). Some TAFs act as direct targets or coactivators for promoter-specific activators while others serve as interfaces for TAF-TAF interactions. Here, we report the molecular cloning, expression and characterization of Drosophila dTAFII60 and its human homolog, hTAFII70. Recombinant TAFII60/70 binds weakly to TBP and tightly to the largest subunit of TFIID, TAFII250. In the presence of TAFII60/70, TBP and TAFII250, a stable ternary complex is formed. Both the human and Drosophila proteins directly interact with another TFIID subunit, dTAFII40. Our findings reveal that Drosophila TAFII60 and human TAFII70 share a high degree of structural similarity and that their interactions with other subunits of TFIID are conserved.

PMC413796 (PMC) (EuropePMC)