Robert E. Collins

TL;DR: These findings couple the function of BHC80 to that of LSD1, and indicate that unmodified H3K4 is part of the ‘histone code’, which raises the possibility that the generation and recognition of the unmodified state on histone tails in general might be just as crucial as post-translational modifications of histone for chromatin and transcriptional regulation.

TL;DR: This review describes structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p) andmethylation of protein arginine residue by PRMTs.

TL;DR: It is shown that ER is directly methylated at lysine 302 (K302) by the SET7 methyltransferase, raising the possibility that generation, recognition, and removal of modifications within the ER hinge region generate "ER modification cassettes" that yield distinct patterns for signaling downstream events.

TL;DR: G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.

TL;DR: It is found that a Phe at the position equivalent to Phe281 of Neurospora crassa DIM-5 or Phe1205 of human G9a allows the enzyme to perform di and tri-methylation, whereas a Tyr at this position is restrictive, inhibiting tri- methylation and thus yielding a mono- or di-MTase.