AF9 Links Histone Acetylation to DOT1L-Mediated H3K79 Methylation

ABSTRACT: The recognition of modified histones by “reader” proteins constitutes a key mechanism regulating gene expression in the chromatin context. Compared with the great variety of readers for histone methylation, few protein modules that recognize histone acetylation are known. Here we show that the evolutionarily conserved YEATS domains constitute a novel family of acetyllysine readers. The human AF9 YEATS domain binds strongly to histone H3K9 acetylation and, to a lesser extent, H3K27 and H3K18 acetylation. Crystal structural studies revealed that AF9 YEATS adopts an eight-stranded immunoglobin fold and utilizes a serine-lined aromatic “sandwiching” cage for acetyllysine readout, representing a novel recognition mechanism that is distinct from that of known acetyllysine readers. Histone acetyl

ORGANISM(S): Homo sapiens

SUBMITTER: Yuanxin Xi 

PROVIDER: E-GEOD-60366 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress