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Molecular Cloning and Expression of the 32-kDa Subunit of Human TFIID Reveals Interactions with VP16 and TFIIB that Mediate Transcriptional Activation

Richard D. Klemm, James A. Goodrich, Sharleen Zhou and Robert Tjian
Proceedings of the National Academy of Sciences of the United States of America
Vol. 92, No. 13 (Jun. 20, 1995), pp. 5788-5792
Stable URL: http://www.jstor.org/stable/2367913
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Molecular Cloning and Expression of the 32-kDa Subunit of Human TFIID Reveals Interactions with VP16 and TFIIB that Mediate Transcriptional Activation
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Abstract

Transcription factor TFIID consists of TATA binding protein (TBP) and at least eight TBP-associated factors (TAFs). As TAFs are required for activated but not basal transcription, we have proposed that TAFs act as coactivators to mediate signals between activators and the basal transcription machinery. Here we report the cloning, expression, and biochemical characterization of the 32-kDa subunit of human (h) TFIID, termed hTAFII32. We find that hTAFII32 is the human homologue of Drosophila TAFII40. In vitro protein-protein interaction assays reveal that as observed with Drosophila TAFII40, hTAFII32 interacts with the C-terminal 39-amino acid activation domain of the acidic transactivator viral protein 16 (VP16) as well as with the general transcription factor TFIIB. Moreover, a partial recombinant TFIID complex containing hTAFII32 was capable of mediating in vitro transcriptional activation by the VP16 activation domain. These findings indicate that specific activator-coactivator interactions have been conserved between human and Drosophila and provide additional support for the function of these interactions in mediating transcriptional activation.

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