共查询到20条相似文献,搜索用时 15 毫秒
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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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GCN5 is a histone acetyltransferase (HAT) essential for development in mammals and critical to stress responses in yeast. The protozoan parasite Toxoplasma gondii is a serious opportunistic pathogen. The study of epigenetics and gene expression in this ancient eukaryote has pharmacological relevance and may facilitate the understanding of these processes in higher eukaryotes. Here we show that the disruption of T. gondii GCN5 yields viable parasites, which were subsequently employed in a proteomics study to identify gene products affected by its loss. Promoter analysis of these TgGCN5-dependent genes, which were mostly parasite specific, reveals a conserved T-rich element. The loss of TgGCN5 does not attenuate virulence in an in vivo mouse model. We also discovered that T. gondii is the only invertebrate reported to date possessing a second GCN5 (TgGCN5-B). TgGCN5-B harbors a strikingly divergent N-terminal domain required for nuclear localization. Despite high homology between the HAT domains, the two TgGCN5s exhibit differing substrate specificities. In contrast to TgGCN5-A, which exclusively targets lysine 18 of H3, TgGCN5-B acetylates multiple lysines in the H3 tail. We also identify two ADA2 homologues that interact differently with the TgGCN5s. TgGCN5-B has the potential to compensate for TgGCN5-A, which probably arose from a gene duplication unique to T. gondii. Our work reveals an unexpected complexity in the GCN5 machinery of this primitive eukaryote. 相似文献
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Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/dGcn5-containing histone acetyltransferase complex in Drosophila
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Guelman S Suganuma T Florens L Swanson SK Kiesecker CL Kusch T Anderson S Yates JR Washburn MP Abmayr SM Workman JL 《Molecular and cellular biology》2006,26(3):871-882
Gcn5 is a conserved histone acetyltransferase (HAT) found in a number of multisubunit complexes from Saccharomyces cerevisiae, mammals, and flies. We previously identified Drosophila melanogaster homologues of the yeast proteins Ada2, Ada3, Spt3, and Tra1 and showed that they associate with dGcn5 to form at least two distinct HAT complexes. There are two different Ada2 homologues in Drosophila named dAda2A and dAda2B. dAda2B functions within the Drosophila version of the SAGA complex (dSAGA). To gain insight into dAda2A function, we sought to identify novel components of the complex containing this protein, ATAC (Ada two A containing) complex. Affinity purification and mass spectrometry revealed that, in addition to dAda3 and dGcn5, host cell factor (dHCF) and a novel SANT domain protein, named Atac1 (ATAC component 1), copurify with this complex. Coimmunoprecipitation experiments confirmed that these proteins associate with dGcn5 and dAda2A, but not with dSAGA-specific components such as dAda2B and dSpt3. Biochemical fractionation revealed that ATAC has an apparent molecular mass of 700 kDa and contains dAda2A, dGcn5, dAda3, dHCF, and Atac1 as stable subunits. Thus, ATAC represents a novel histone acetyltransferase complex that is distinct from previously purified Gcn5/Pcaf-containing complexes from yeast and mammalian cells. 相似文献
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Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo 总被引:7,自引:0,他引:7
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Martinez E Palhan VB Tjernberg A Lymar ES Gamper AM Kundu TK Chait BT Roeder RG 《Molecular and cellular biology》2001,21(20):6782-6795
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A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing 总被引:3,自引:0,他引:3
Zhao Y Lang G Ito S Bonnet J Metzger E Sawatsubashi S Suzuki E Le Guezennec X Stunnenberg HG Krasnov A Georgieva SG Schüle R Takeyama K Kato S Tora L Devys D 《Molecular cell》2008,29(1):92-101