GSBS Student Publications

Title

A conserved Swi2/Snf2 ATPase motif couples ATP hydrolysis to chromatin remodeling

UMMS Affiliation

Graduate School of Biomedical Sciences; Program in Molecular Medicine; Program in Gene Function and Expression

Date

7-1-2005

Document Type

Article

Medical Subject Headings

Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Animals; Chromatin Assembly and Disassembly; Conserved Sequence; DNA-Binding Proteins; Histones; Humans; Hydrolysis; Molecular Sequence Data; Nucleosomes; Transcription Factors

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: Mol Cell Biol. 2005 Jul;25(14):5880-92. Link to article on publisher's site

DOI of Published Version

10.1128/MCB.25.14.5880-5892.2005

Related Resources

Link to Article in PubMed

Journal Title

Molecular and cellular biology

PubMed ID

15988005