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Molecular and Cellular Biology, November 1998, p. 6293-6304, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Persistent Interactions of Core Histone Tails with Nucleosomal DNA following Acetylation and Transcription Factor Binding

Vesco Mutskov,1,dagger Delphine Gerber,2 Dimitri Angelov,3,dagger Juan Ausio,4 Jerry Workman,5 and Stefan Dimitrov2,*

Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia,1 and Institute of Solid State Physics, Bulgarian Academy of Sciences, 1784 Sofia,3 Bulgaria; Laboratoire d'Etudes de la Différenciation et l'Adhérence Cellulaires, UMR CNRS/UJF 5538, Institut Albert Bonniot, 38706 La Tronche Cedex, France2; Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada4; and Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 168025

Received 18 March 1998/Returned for modification 24 April 1998/Accepted 31 July 1998

In this study, we examined the effect of acetylation of the NH2 tails of core histones on their binding to nucleosomal DNA in the absence or presence of bound transcription factors. To do this, we used a novel UV laser-induced protein-DNA cross-linking technique, combined with immunochemical and molecular biology approaches. Nucleosomes containing one or five GAL4 binding sites were reconstituted with hypoacetylated or hyperacetylated core histones. Within these reconstituted particles, UV laser-induced histone-DNA cross-linking was found to occur only via the nonstructured histone tails and thus presented a unique tool for studying histone tail interactions with nucleosomal DNA. Importantly, these studies demonstrated that the NH2 tails were not released from nucleosomal DNA upon histone acetylation, although some weakening of their interactions was observed at elevated ionic strengths. Moreover, the binding of up to five GAL4-AH dimers to nucleosomes occupying the central 90 bp occurred without displacement of the histone NH2 tails from DNA. GAL4-AH binding perturbed the interaction of each histone tail with nucleosomal DNA to different degrees. However, in all cases, greater than 50% of the interactions between the histone tails and DNA was retained upon GAL4-AH binding, even if the tails were highly acetylated. These data illustrate an interaction of acetylated or nonacetylated histone tails with DNA that persists in the presence of simultaneously bound transcription factors.

* Corresponding author. Mailing address: Laboratoire d'Etudes de la Différenciation et de l'Adhérence Cellulaires, UMR CNRS/UJF 5538, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche Cedex, France. Phone: (33) 4 76 54 94 73. Fax: (33) 4 76 54 94 25. E-mail: Stefan.Dimitrov{at}ujf-grenoble.fr.

dagger Present address: Laboratoire d'Etudes de la Différenciation et l'Adhérence Cellulaires, UMR CNRS/UJF 5538, Institut Albert Bonniot, 38706 La Tronche Cedex, France.

Molecular and Cellular Biology, November 1998, p. 6293-6304, Vol. 18, No. 11
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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