A novel histone fold domain-containing protein that replaces TAF6 in Drosophila SAGA is required for SAGA-dependent gene expression.
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.
Mesh Terms:
Animals, Drosophila Proteins, Drosophila melanogaster, Gene Expression Regulation, Histone Acetyltransferases, Mutation, Peptides, Protein Binding, Protein Folding, TATA-Binding Protein Associated Factors, Transcription Factor TFIID, Transcription Factors
Animals, Drosophila Proteins, Drosophila melanogaster, Gene Expression Regulation, Histone Acetyltransferases, Mutation, Peptides, Protein Binding, Protein Folding, TATA-Binding Protein Associated Factors, Transcription Factor TFIID, Transcription Factors
Genes Dev.
Date: Dec. 15, 2009
PubMed ID: 20008933
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