The yeast SNF2/SWI2 protein has DNA-stimulated ATPase activity required for transcriptional activation

B. C. Laurent, I. Treich, M. Carlson

Research output: Contribution to journalArticlepeer-review

251 Scopus citations

Abstract

The yeast SNF2 (SWI2) protein functions with SNF5, SNF6, SWI1, and SWI3 in the transcriptional activation of many differently regulated genes. These proteins appear to facilitate activation by gene-specific regulatory proteins. SNF2 is highly conserved among eukaryotes and defines a family of proteins with similarity to helicases and nucleic acid-dependent NTPases. Here, we present genetic and biochemical evidence that SNF2 has DNA-stimulated ATPase activity. Mutations in the nucleoside triphosphate (NTP)-binding motif and other conserved motifs impair SNF2 function. Swapping experiments with another member of this family indicate that the helicase-related domains are functionally interchangeable. Finally, bacterially expressed SNF2 protein has ATPase activity that is stimulated by double-stranded DNA, and mutation of the NTP-binding site abolishes this activity. Deletion analysis shows that the helicase-like region of SNF2 is necessary, but not sufficient, for transcriptional activation.

Original languageEnglish
Pages (from-to)583-591
Number of pages9
JournalGenes and Development
Volume7
Issue number4
DOIs
StatePublished - 1993
Externally publishedYes

Keywords

  • ATP hydrolysis
  • Chromatin
  • S cerevisiae
  • SNF2/SWI2 protein
  • Transcriptional activation

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