A novel histone fold domain-containing protein that replaces TAF6 in Drosophila SAGA is required for SAGA-dependent gene expression

Genes Dev. 2009 Dec 15;23(24):2818-23. doi: 10.1101/gad.1846409.

Abstract

The histone acetyltransferase complex SAGA is well characterized as a coactivator complex in yeast. In this study of Drosophila SAGA (dSAGA), we describe three novel components that include an ortholog of Spt20, a potential ortholog of Sgf73/ATXN7, and a novel histone fold protein, SAF6 (SAGA factor-like TAF6). SAF6, which binds directly to TAF9, functions analogously in dSAGA to TAF6/TAF6L in the yeast and human SAGA complexes, respectively. Moreover, TAF6 in flies is restricted to TFIID. Mutations in saf6 disrupt SAGA-regulated gene expression without disrupting acetylated or ubiquitinated histone levels. Thus, SAF6 is essential for SAGA coactivator function independent of the enzymatic activities of the complex.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / enzymology*
  • Drosophila melanogaster / genetics
  • Gene Expression Regulation*
  • Histone Acetyltransferases / genetics
  • Histone Acetyltransferases / metabolism*
  • Mutation / genetics
  • Peptides / isolation & purification
  • Protein Binding
  • Protein Folding
  • TATA-Binding Protein Associated Factors / metabolism*
  • Transcription Factor TFIID / metabolism*
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*

Substances

  • Drosophila Proteins
  • Peptides
  • SAF6 protein, Drosophila
  • TATA-Binding Protein Associated Factors
  • Taf6 protein, Drosophila
  • Transcription Factor TFIID
  • Transcription Factors
  • Histone Acetyltransferases