Transcriptional activators direct histone acetyltransferase complexes to nucleosomes

Rhea T. Utley, Keiko Ikeda, Patrick A. Grant, Jacques Côté, David J. Steger, Anton Eberharter, Sam John and Jerry L. Workman ()
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Rhea T. Utley: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Keiko Ikeda: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Patrick A. Grant: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Jacques Côté: Laval University Cancer Research Center
David J. Steger: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Anton Eberharter: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Sam John: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University
Jerry L. Workman: Howard Hughes Medical Institute, 306 Althouse Laboratory, Pennsylvania State University

Nature, 1998, vol. 394, issue 6692, 498-502

Abstract: Abstract Transcriptional co-activators were originally identified as proteins that act as intermediaries between upstream activators and the basal transcription machinery. The discovery that co-activators such as Tetrahymena and yeast Gcn51,2, as well as human p300/CBP3,4, pCAF5, Src-16, ACTR7 and TAFII2508, can acetylate histones suggests that activators may be involved in targeting acetylation activity to promoters. Several histone deacetylases have been linked to transcriptional co-repressor proteins9, suggesting that the action of both acetylases and deacetylases is important in the regulation of many genes. Here we demonstrate the binding of two native yeast histone acetyltransferase (HAT) complexes to the herpesvirus VP16 activation domain and the yeast transcriptional activator Gcn4, and show that it is their interaction with the VP16 activation domain that targets Gal4–VP16-bound nucleosomes for acetylation. We find that Gal4–VP16-driven transcription from chromatin templates is stimulated by both HAT complexes in an acetyl CoA-dependent reaction. Our results demonstrate the targeting of native HAT complexes by a transcription-activation domain to nucleosomes in order to activate transcription.

Date: 1998
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DOI: 10.1038/28886

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