The C-terminal domains of ADA2 proteins determine selective incorporation into GCN5-containing complexes that target histone H3 or H4 for acetylation

FEBS Letters

Volumn 586, Issue 19, 2012, Pages 3279-3286

  E Vamos, Edith ^a   Boros, Imre M ^a,b  

^a UNIVERSITY OF SZEGED   (Hungary)

^b INSTITUTE OF BIOCHEMISTRY   (Hungary)

Author keywords

ADA2; ATAC complex; GCN5 KAT2; Histone acetylation; SAGA complex

Indexed keywords

ADAPTOR PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE GCN5; HISTONE H3; HISTONE H4; PROTEIN ADA2; PROTEIN ATAC; TRANSCRIPTION FACTOR SAGA; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; HISTONE ACETYLATION; IN VIVO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN TARGETING;

ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; ANIMALS, GENETICALLY MODIFIED; CELL LINE; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; GENES, INSECT; HISTONE ACETYLTRANSFERASES; HISTONES; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; MUTATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER;

DROSOPHILA MELANOGASTER; METAZOA;

EID: 84866601659     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.06.051     Document Type: Article

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