The C-terminal domains of ADA2 proteins determine selective incorporation into GCN5-containing complexes that target histone H3 or H4 for acetylation |
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Authors: | Edith E Vamos Imre M Boros |
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Affiliation: | a Department of Biochemistry and Molecular Biology, University of Szeged, Közép fasor 52, H-6726 Szeged, Hungary b Institute of Biochemistry, Biological Research Center, Temesvári krt. 62, H-6726 Szeged, Hungary |
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Abstract: | 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. |
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Keywords: | Histone acetylation ADA2 SAGA complex ATAC complex GCN5 KAT2 |
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