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Science 7 July 1995:
Vol. 269. no. 5220, pp. 75 - 78
DOI: 10.1126/science.7604282
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Articles

Science, Vol 269, Issue 5220, 75-78
Copyright © 1995 by American Association for the Advancement of Science

articles

The TBP-TFIIA interaction in the response to acidic activators in vivo

LA Stargell and K Struhl

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.


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