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Updated: Oct 6, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator
R O Weinzierl1, B D Dynlacht, R Tjian
1Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Abstract:
The TFIID complex consists of the TATA-binding protein (TBP) and associated factors (TAFs) serving to mediate transcriptional activation by promoter-specific regulators. Here we report the cloning of Drosophila TAFII250 and the assembly of a partial complex containing recombinant TBP, TAFII110 and the C-terminal domain of TAFII250. This triple complex supports Sp1 activation and reveals specific interactions between TAFII250, TBP and TAFII110.
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