title: Sound of silence: the properties and functions of repressive Lys methyltransferases.
abstract: The methylation of histone Lys residues by Lys methyltransferases (KMTs) regulates chromatin organization and either activates or represses gene expression, depending on the residue that is targeted. KMTs are emerging as key components in several cellular processes, and their deregulation is often associated with pathogenesis. Here, we review the current knowledge on the main KMTs that are associated with gene silencing: namely, those responsible for methylating histone H3 Lys 9 (H3K9), H3K27 and H4K20. We discuss their biochemical properties and the various mechanisms by which they are targeted to the chromatin and regulate gene expression, as well as new data on the interplay between them and other chromatin modifiers.
authors.affiliation: 1] Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR7216 CNRS, Paris, France. [2] National Research Council (CNR), Institute of Cell Biology and Neurobiology (IBCN), 00143 Rome, Italy.
authors.forename: Chiara
authors.initials: C
authors.lastname: Mozzetta
authors.affiliation: Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR7216 CNRS, Paris, France.
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Boyarchuk
authors.affiliation: Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR7216 CNRS, Paris, France.
authors.forename: Julien
authors.initials: J
authors.lastname: Pontis
authors.affiliation: Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR7216 CNRS, Paris, France.
authors.forename: Slimane
authors.initials: S
authors.lastname: Ait-Si-Ali
mesh_terms: D000818:Animals; D042002:Chromatin Assembly and Disassembly; D020868:Gene Silencing; D011495:Histone-Lysine N-Methyltransferase / Q000502:physiology*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones; D011495:Histone-Lysine N-Methyltransferase