Nucleic Acids Research, Vol 24, Issue 19 3685-3692, Copyright © 1996 by Oxford University Press
E Richmond and CL Peterson
The yeast SWI2/SNF2 polypeptide is a subunit of the SWI/SNF protein complex
that is required for many transcriptional activators to function in a
chromatin context. SWI2 is believed to be the founding member of a new
subfamily of DNA-stimulated ATPases/DNA helicases that includes proteins
that function in DNA repair (RAD5, RAD16, ERCC6), recombination (RAD54),
transcription (MOT1, ISWI, brm, BRG1, hBRM) and cell cycle control (STH1).
We have created a set of 16 mutations within the SWI2 ATPase domain and
have analyzed the functional consequences of these mutations in vivo. We
have identified residues within each of the seven ATPase motifs that are
required for SWI2 function. We have also identified crucial residues that
are interspersed between the known ATPase motifs. In contrast, we identify
other highly conserved residues that appear to be dispensable for SWI2
function. We also find that single amino acid changes in ATPase motifs IV
and VI lead to a dominant negative phenotype. None of the 12 SWI2 mutations
that disrupt SWI2 activity in vivo alter the assembly of the SWI/SNF
complex. These studies provide an invaluable framework for biochemical
analysis of the SWI2 ATPase and for functional analysis of other SWI2
family members.
ARTICLES
Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2
Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester 01605, USA.
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