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J. Biol. Chem., Vol. 281, Issue 26, 18126-18134, June 30, 2006

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The Swi2/Snf2 Bromodomain Is Required for the Displacement of SAGA and the Octamer Transfer of SAGA-acetylated Nucleosomes^*

Ahmed H. Hassan¹, Salma Awad, and Philippe Prochasson

From the Faculty of Medicine and Health Sciences, Department of Biochemistry, United Arab Emirates University, P. O. Box 17666, Al-Ain, United Arab Emirates and the Stowers Institute for Medical Research, Kansas City, Missouri 64110

The SWI/SNF and SAGA chromatin-modifying complexes contain bromodomains that help anchor these complexes to acetylated promoter nucleosomes. To study the importance of bromodomains in these complexes, we have compared the chromatin-remodeling and octamer-transfer activity of the SWI/SNF complex to a mutant complex that lacks the Swi2/Snf2 bromodomain. Here we show that the SWI/SNF complex can remodel or transfer SAGA-acetylated nucleosomes more efficiently than the Swi2/Snf2 bromodomain-deleted complex. These results demonstrate that the Swi2/Snf2 bromodomain is important for the remodeling as well as for the octamer-transfer activity of the complex on H3-acetylated nucleosomes. Moreover, we show that, although the wild-type SWI/SNF complex displaces SAGA that is bound to acetylated nucleosomes, the bromodomain mutant SWI/SNF complex is less efficient in SAGA displacement. Thus, the Swi2/Snf2 bromodomain is required for the full functional activity of SWI/SNF on acetylated nucleosomes and is important for the displacement of SAGA from acetylated promoter nucleosomes.

Received for publication, March 27, 2006 , and in revised form, April 26, 2006.

^* This work was supported by grants from the faculty of Medicine and Health Sciences (Grant NP/05/16) and Terry Fox Funds for Cancer Research (to A. H. H.) and by a Leukemia and Lymphoma Society fellowship (to P. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Faculty of Medicine and Health Sciences, Dept. of Biochemistry, UAE University, P. O. Box 17666, Al-Ain, United Arab Emirates. Tel.: 971-3-713-7478; Fax: 971-3-767-2033; E-mail: ahmedh{at}uaeu.ac.ae.

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