The C‐terminal domains of ADA2 proteins determine selective incorporation into GCN5‐containing complexes that target histone H3 or H4 for acetylation
Copyright policy )The C‐terminal domains of ADA2 proteins determine selective incorporation into GCN5‐containing complexes that target histone H3 or H4 for acetylation
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.
- University of Szeged Hungary
- MTA Biological Research Centre Hungary
- Institute of Biochemistry Hungary
Recombinant Fusion Proteins, Molecular Sequence Data, SAGA complex, Acetylation, Genes, Insect, ADA2, Protein Structure, Secondary, Cell Line, Animals, Genetically Modified, Histones, GCN5 KAT2, Drosophila melanogaster, Histone acetylation, Multiprotein Complexes, Mutation, Animals, Drosophila Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, RNA, Messenger, ATAC complex, Histone Acetyltransferases
Recombinant Fusion Proteins, Molecular Sequence Data, SAGA complex, Acetylation, Genes, Insect, ADA2, Protein Structure, Secondary, Cell Line, Animals, Genetically Modified, Histones, GCN5 KAT2, Drosophila melanogaster, Histone acetylation, Multiprotein Complexes, Mutation, Animals, Drosophila Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, RNA, Messenger, ATAC complex, Histone Acetyltransferases
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