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Molecular and Cellular Biology, September 1999, p. 5952-5959, Vol. 19, No. 9
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Histone Acetyltransferase Complexes Can Mediate Transcriptional Activation by the Major Glucocorticoid Receptor Activation Domain

Annika E. Wallberg,1,* Kristen E. Neely,2 Jan-Åke Gustafsson,1 Jerry L. Workman,2 Anthony P. H. Wright,1,3 and Patrick A. Grant2

Karolinska Institute, Department of Biosciences, NOVUM, S-14157 Huddinge,1 and Södertörns Högskola, S-14104 Huddinge,3 Sweden, and Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802-45002

Received 18 February 1999/Returned for modification 15 April 1999/Accepted 18 June 1999

Previous studies have shown that the Ada adapter proteins are important for glucocorticoid receptor (GR)-mediated gene activation in yeast. The N-terminal transactivation domain of GR, tau 1, is dependent upon Ada2, Ada3, and Gcn5 for transactivation in vitro and in vivo. Using in vitro techniques, we demonstrate that the GR-tau 1 interacts directly with the native Ada containing histone acetyltransferase (HAT) complex SAGA but not the related Ada complex. Mutations in tau 1 that reduce tau 1 transactivation activity in vivo lead to a reduced binding of tau 1 to the SAGA complex and conversely, mutations increasing the transactivation activity of tau 1 lead to an increased binding of tau 1 to SAGA. In addition, the Ada-independent NuA4 HAT complex also interacts with tau 1. GAL4-tau 1-driven transcription from chromatin templates is stimulated by SAGA and NuA4 in an acetyl coenzyme A-dependent manner. Low-activity tau 1 mutants reduce SAGA- and NuA4-stimulated transcription while high-activity tau 1 mutants increase transcriptional activation, specifically from chromatin templates. Our results demonstrate that the targeting of native HAT complexes by the GR-tau 1 activation domain mediates transcriptional stimulation from chromatin templates.

* Corresponding author. Mailing address: Karolinska Institute, Department of Biosciences, NOVUM, S-14157 Huddinge, Sweden. Phone: 46-8-6089155. Fax: 46-8-7745538. E-mail: annika.wallberg{at}csb.ki.se.

Molecular and Cellular Biology, September 1999, p. 5952-5959, Vol. 19, No. 9
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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