Ontology highlight
ABSTRACT:
SUBMITTER: Zhang Q
PROVIDER: S-EPMC5014688 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20160818 9
Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that crotonyl-lysine of histone H3 lysine 18 is engulfed deep in an aromatic cage of the YEATS domain w ...[more]