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The C‐terminal domains of ADA2 proteins determine selective incorporation into GCN5‐containing complexes that target histone H3 or H4 for acetylation
Author(s) -
E. Vamos Edith,
Boros Imre M.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.051
Subject(s) - acetylation , histone , histone acetyltransferase , histone h4 , histone h3 , histone h1 , drosophila melanogaster , histone methyltransferase , biology , microbiology and biotechnology , protein subunit , histone code , histone h2a , sap30 , biochemistry , nucleosome , gene
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.