Scientists from the University of Texas MD Anderson Cancer Center have demonstrated that histone protein could play its role through the protein reader called YEATS. YEATS could be absorbed to the tail of histone protein and plays important role in gene activating. This study was published in Cell.

The histone proteins are subjected to a number of posttranslational modifications(PTMs) that play a critical role in regulating chromatin dynamics and the accessibility of the underlying DNA in eukaryotes. The recognition of modified histones by “reader” proteins constitutes a key mechanism regulating gene expression in the chromatin context. Compared with the understanding of protein modules known to recognize histone methylation, our knowledge of the protein modules that can recognize histone acetylation is very limited.

In this study, researchers have reported the discovery of the YEAS domains as a novel family of histone acetylation readers. They found that YEATS domains of AF9 from diverse species all bind to acetylation (H3K9ac). ChIP-seq experiments revealed a strong colocalization of AF9 and H3K9 acetylation genome-wide, which is important for the chromatin recruitment of the H3K79 methyltransferase DOT1L.

Their studies also identified the evolutionarily conserved YEATS domain as a novel acetyllysine-binding module and established a direct link between histone acetylation and DOT1L-mediated H3K79 methylation in transcription control.

Reference:

Li Y, Wen H, Xi Y, et al. AF9 YEATS Domain Links Histone Acetylation to DOT1L-Mediated H3K79 Methylation[J]. Cell, 2014, 159(3): 558-571.