FlyBase Reference Report: Weake et al., 2009, Genes Dev. 23(24): 2818--2823

Reference

Citation

Weake, V.M., Swanson, S.K., Mushegian, A., Florens, L., Washburn, M.P., Abmayr, S.M., Workman, J.L. (2009). A novel histone fold domain-containing protein that replaces TAF6 in Drosophila SAGA is required for SAGA-dependent gene expression. Genes Dev. 23(24): 2818--2823.

FlyBase ID

FBrf0209543

Publication Type

Research paper

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.

PubMed ID

20008933

PubMed Central ID

PMC2800089 (PMC) (EuropePMC)

DOI

10.1101/gad.1846409

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