Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes

Laurie A. Boyer, Michael R. Langer, Kimberly A. Crowley, Song Tan, John M. Denu, Craig L. Peterson

Research output: Contribution to journalArticlepeer-review

174 Scopus citations

Abstract

The SANT domain is a novel motif found in a number of eukaryotic transcriptional regulatory proteins that was identified based on its homology to the DNA binding domain of c-myb. Here we show that the SANT domain is essential for the in vivo functions of yeast Swi3p, Ada2p, and Rsc8p, subunits of three distinct chromatin remodeling complexes. We also find that the Ada2p SANT domain is essential for histone acetyltransferase activity of native, Gcn5p-containing HAT complexes. Furthermore, kinetic analyses indicate that an intact SANT domain is required for an Ada2p-dependent enhancement of histone tail binding and enzymatic catalysis by Gcn5p. Our results are consistent with a general role for SANT domains in functional interactions with histone N-terminal tails.

Original languageEnglish (US)
Pages (from-to)935-942
Number of pages8
JournalMolecular cell
Volume10
Issue number4
DOIs
StatePublished - Oct 1 2002

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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