A novel histone fold domain-containing protein that replaces TAF6 in Drosophila SAGA is required for SAGA-dependent gene expression.
[No authors listed]
摘要
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.
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基因功能
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基因
Trf2, Ada1-2, CG9689, e(y)1, Spt7, Ada3, Taf8, Saf6, Pex12, Atxn7, Taf10b, Taf10, Trf, Taf11, CG5390, Taf13, Nipped-A, Oda, Obp56a, Sgf29, Tbp, Gp150, ImpE2, lqf, Taf2, Gcn5, Spt20, Taf4, not, Sgf11, Taf6, mia, kra, Osi6, Taf1, Taf7, Ada2b, Calr, Taf12, Spt3, CG4702, Sap47, wda, bip2, bsk, e(y)2, Taf5
原始数据
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文献解读
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