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ADA2 adaptor proteins are essential subunits of GCN5-containing histone acetyltransferase (HAT) complexes. In metazoa ADA2a is present in the histone H4-specific ATAC, and ADA2b in the histone H3-specific SAGA complex. Using domain-swapped ADA2 chimeras, we determined that the in vivo function of Drosophila melanogaster SAGA and ATAC HAT complexes depend on the C-terminal region of the ADA2 subunit they contain. Our findings demonstrate that the ADA2 C-terminal regions play an important role in the specific incorporation of ADA2 into SAGA- or ATAC-type complexes, which in turn determines H3- or H4-specific histone targeting. 相似文献
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Xin Liu Wei Xiao Xu-Dong Wang Yue-Fang Li Jiahuai Han Yingqiu Li 《The Journal of biological chemistry》2013,288(51):36648-36661
p38-interacting protein (p38IP) is a component of the GCN5 histone acetyltransferase-containing coactivator complex (GCN5-SAGA complex). It remains unclear whether p38IP or GCN5-SAGA is involved in cell cycle regulation. Using RNA interference to knock down p38IP, we observed that cells were arrested at the G2/M phase, exhibiting accumulation of cyclins, shrunken spindles, and hypoacetylation of α-tubulin. Further analysis revealed that knockdown of p38IP led to proteasome-dependent degradation of GCN5. GCN5 associated with and acetylated α-tubulin, and recovering GCN5 protein levels in p38IP knockdown cells by ectopic expression of GCN5 efficiently reversed α-tubulin hypoacetylation and G2/M arrest. During the G2/M transition, the association of α-tubulin with GCN5 increased, and the acetylation of α-tubulin reached a peak. Biochemical analyses demonstrated that the interaction between p38IP and GCN5 depended on the p38IP N terminus (1–381 amino acids) and GCN5 histone acetyltransferase domain and bromodomain. The p38IP N terminus could effectively reverse p38IP depletion-induced GCN5 degradation, thus recovering α-tubulin acetylation and G2/M progression. p38IP-mediated suppression of GCN5 ubiquitination most likely occurs via nuclear sequestration of GCN5. Our data indicate that the GCN5-SAGA complex is required for G2/M progression, mainly because p38IP promotes the acetylation of α-tubulin by preventing the degradation of GCN5, in turn facilitating the formation of the mitotic spindle. 相似文献
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Aida M Beis D Heidstra R Willemsen V Blilou I Galinha C Nussaume L Noh YS Amasino R Scheres B 《Cell》2004,119(1):109-120
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Two Arabidopsis orthologs of the transcriptional coactivator ADA2 have distinct biological functions
Amy T. Hark Konstantinos E. Vlachonasios Kanchan A. Pavangadkar Sumana Rao Hillary Gordon Ioannis-Dimosthenis Adamakis Athanasios Kaldis Michael F. Thomashow Steven J. Triezenberg 《Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms》2009,1789(2):117-124