Nicolas Lacoste

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: It is shown that the Dot1 protein possesses intrinsic histone methyltransferase activity, and it is demonstrated that, like its mammalian homolog PRMT1, Rmt1 specifically dimethylates an arginine residue at position 3 of histone H4 N-terminal tail.

TL;DR: Results indicate that the essential aspect of Esa1 and Epl1 resides in picNuA4 function, and propose that picNUA4 represents a nontargeted histone H4/H2A acetyltransferase activity responsible for global acetylation, whereas the NuA4 complex is recruited to specific genomic loci to perturb locally the dynamic acetylated/deacetylation equilibrium.

TL;DR: It is shown that histone H4 N-terminal domain, unlike other histone tails, interacts with Dot1 and is essential for H3 K79 methylation, and that the heterochromatin protein Sir3 inhibits Dot1-mediated methylation and that this inhibition is dependent on lysine 16 of H4.

TL;DR: The impact of NuA4-dependent acetylation on SWR1-driven incorporation of H2A.Z into chromatin is investigated, and depletion experiments indicate that the bromodomain-containing protein Bdf1 is important for NuA 4-dependent stimulation ofSWR1.