A conserved Swi2/Snf2 ATPase motif couples ATP hydrolysis to chromatin remodeling
Graduate School of Biomedical Sciences; Program in Molecular Medicine; Program in Gene Function and Expression
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
Life Sciences | Medicine and Health Sciences
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.
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Citation: Mol Cell Biol. 2005 Jul;25(14):5880-92. Link to article on publisher's site
Molecular and cellular biology
Smith, Corey Lewis and Peterson, Craig L., "A conserved Swi2/Snf2 ATPase motif couples ATP hydrolysis to chromatin remodeling" (2005). GSBS Student Publications. 1130.