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Recognition of nucleosome substrates by chromatin enzymes
Author(s) -
Tan Song,
Hnatkovich Brian,
Irvine James,
Selleck William,
Sermwittayawong Decha
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a39
Subject(s) - nucleosome , histone acetyltransferase , chromatin , microbiology and biotechnology , histone , histone code , chromatin remodeling , biology , acetylation , chemistry , biochemistry , genetics , dna , gene
While we possess a good understanding of how transcription factors bind to their DNA targets, we lack equivalent biochemical or structural insight into how chromatin factors bind to their nucleosome substrate. To address this deficiency, we are studying how transcription factors and chromatin enzymes interact with nucleosomes. Our studies of histone acetyltransferase chromatin modification enzymes shows that although the yeast histone Gcn5 and Esa1 acetyltransferase subunits can modify histone substrates, neither acetylates the physiological nucleosome substrate efficiently. In contrast, the parent megadalton, multicomponent SAGA and NuA4 complexes possess strong nucleosome acetyltransferase activity. We have identified minimal catalytic SAGA and NuA4 subcomplexes sufficient and necessary to acetylate nucleosomes. Deletion analysis of the catalytic NuA4 subcomplex, Piccolo NuA4 (comprised of the Epl1, Yng2 and Esa1 subunits) identifies the Epl1 EPcA homology region and the Esa1 chromodomain as critical for Piccolo's ability to specifically act on nucleosomes.