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Molecular and Cellular Biology, July 2005, p. 5880-5892, Vol. 25, No. 14
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.14.5880-5892.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Conserved Swi2/Snf2 ATPase Motif Couples ATP Hydrolysis to Chromatin Remodeling

Corey L. Smith and Craig L. Peterson*

Program in Molecular Medicine, Interdisciplinary Graduate Program, University of Massachusetts Medical School, Worcester, Massachusetts 01605

Received 1 March 2005/ Returned for modification 6 April 2005/ Accepted 29 April 2005

Yeast (Saccharomyces cerevisiae) SWI/SNF is a prototype for a large family of ATP-dependent chromatin-remodeling enzymes that facilitate numerous DNA-mediated processes. Swi2/Snf2 is the catalytic subunit of SWI/SNF, and it is the founding member of a novel subfamily of the SF2 superfamily of DNA helicase/ATPases. Here we present a functional analysis of the diagnostic set of helicase/ATPase sequence motifs found within all Swi2p/Snf2p family members. Whereas many of these motifs play key roles in ATP binding and/or hydrolysis, we identify residues within conserved motif V that are specifically required to couple ATP hydrolysis to chromatin-remodeling activity. Interestingly, motif V of the human Swi2p/Snf2p homolog, Brg1p, has been shown to be a possible hot spot for mutational alterations associated with cancers.

* Corresponding author. Mailing address: University of Massachusetts Medical School, Program in Molecular Medicine, Biotech 2, Suite 210, Worcester, MA 01605. Phone: (508) 856-5858. Fax: (508) 856-5011. E-mail: Craig.Peterson{at}umassmed.edu.

Molecular and Cellular Biology, July 2005, p. 5880-5892, Vol. 25, No. 14
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.14.5880-5892.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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