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Molecular and Cellular Biology, October 1998, p. 5861-5867, Vol. 18, No. 10
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

ADR1-Mediated Transcriptional Activation Requires the Presence of an Intact TFIID Complexdagger

Philip B. Komarnitsky,1 Edward R. Klebanow,2 P. Anthony Weil,2 and Clyde L. Denis1,*

Department of Biochemistry and Molecular Biology, University of New Hampshire, Durham, New Hampshire 03824,1 and Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-06152

Received 22 April 1998/Returned for modification 15 June 1998/Accepted 25 June 1998

The yeast transcriptional activator ADR1, which is required for ADH2 and other genes' expression, contains four transactivation domains (TADs). While previous studies have shown that these TADs act through GCN5 and ADA2, and presumably TFIIB, other factors are likely to be involved in ADR1 function. In this study, we addressed the question of whether TFIID is also required for ADR1 action. In vitro binding studies indicated that TADI of ADR1 was able to retain TAFII90 from yeast extracts and TADII could retain TBP and TAFII130/145. TADIV, however, was capable of retaining multiple TAFIIs, suggesting that TADIV was binding TFIID from yeast whole-cell extracts. The ability of TADIV truncation derivatives to interact with TFIID correlated with their transcription activation potential in vivo. In addition, the ability of LexA-ADR1-TADIV to activate transcription in vivo was compromised by a mutation in TAFII130/145. ADR1 was found to associate in vivo with TFIID in that immunoprecipitation of either TAFII90 or TBP from yeast whole-cell extracts specifically coimmunoprecipitated ADR1. Most importantly, depletion of TAFII90 from yeast cells dramatically reduced ADH2 derepression. These results indicate that ADR1 physically associates with TFIID and that its ability to activate transcription requires an intact TFIID complex.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Rudman Hall, University of New Hampshire, Durham, NH 03824. Phone: (603) 862-2427. Fax: (603) 862-4013. E-mail: cldenis{at}christa.unh.edu.

dagger Scientific contribution 1993 from the New Hampshire Agricultural Experiment Station.

Molecular and Cellular Biology, October 1998, p. 5861-5867, Vol. 18, No. 10
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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