Kay L. Walter

TL;DR: A novel class of methylated H3K4 effector domains—the PHD domains of the ING (for inhibitor of growth) family of tumour suppressor proteins—are identified and established a pivotal role for trimethylation of H 3K4 in gene repression and, potentially, tumour suppressing mechanisms.

TL;DR: The structure of the mouse ING2 PHD finger in complex with a histone H3 peptide trimethylated at lysine 4 is reported and strong binding of other ING and YNG PHD fingers suggests that the recognition of H3K4me3 histone code is a general feature of the ING/YNG proteins.

TL;DR: In this article, a plant homeodomain (PHD) finger bound to histone H3 trimethylated at lysine 4 (H3K4me3) was found to be essential for the recognition of histone methylation in mammalian DNA recombination.

TL;DR: In this paper, the histone methyl-lysine binding activity of PHD fingers has been investigated in the Saccharomyces cerevisiae proteome and shown to constitute a general class of effector modules for histone trimethylation.

TL;DR: It is shown that Yng1p interacts with the amino-terminal tail of histone H3 and that this interaction can be disrupted by loss of lysine 4 methylation within this tail, and a novel function is identified for the Yng 1p PHD finger in promoting stabilization of the NuA3 complex at chromatin through recognition of hist one H3 lysined4 methylation.