title: The methyltransferase Suv39h1 links the SUMO pathway to HP1α marking at pericentric heterochromatin.
abstract: The trimethylation of histone H3 on lysine 9 (H3K9me3) - a mark recognized by HP1 that depends on the Suv39h lysine methyltransferases (KMTs) - has provided a basis for the reader/writer model to explain HP1 accumulation at pericentric heterochromatin in mammals. Here, we identify the Suv39h1 paralog, as a unique enhancer of HP1α sumoylation both in vitro and in vivo. The region responsible for promoting HP1α sumoylation (aa1-167) is distinct from the KMT catalytic domain and mediates binding to Ubc9. Tethering the 1-167 domain of Suv39h1 to pericentric heterochromatin, but not mutants unable to bind Ubc9, accelerates the de novo targeting of HP1α to these domains. Our results establish an unexpected feature of Suv39h1, distinct from the KMT activity, with a major role for heterochromatin formation. We discuss how linking Suv39h1 to the SUMO pathway provides conceptual implications for our general view on nuclear domain organization and physiological functions.
authors.affiliation: Institut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, F-75005 Paris, France.|Sorbonne Universités, UPMC Université Paris 06, CNRS, UMR3664, F-75005 Paris, France.
authors.forename: Christèle
authors.initials: C
authors.lastname: Maison
authors.affiliation: Institut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, F-75005 Paris, France.|Sorbonne Universités, UPMC Université Paris 06, CNRS, UMR3664, F-75005 Paris, France.
authors.forename: Delphine
authors.initials: D
authors.lastname: Bailly
authors.affiliation: Institut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, F-75005 Paris, France.|Sorbonne Universités, UPMC Université Paris 06, CNRS, UMR3664, F-75005 Paris, France.
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Quivy
authors.affiliation: Institut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, F-75005 Paris, France.|Sorbonne Universités, UPMC Université Paris 06, CNRS, UMR3664, F-75005 Paris, France.
authors.forename: Geneviève
authors.initials: G
authors.lastname: Almouzni
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D000090266:Chromobox Protein Homolog 5; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D006570:Heterochromatin / Q000378:metabolism*; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D008954:Models, Biological; D041681:NIH 3T3 Cells; D011485:Protein Binding; D000072417:Protein Domains; D021381:Protein Transport; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D058207:Sumoylation; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism; D000098843:Ubiquitin-Conjugating Enzyme UBC9
chemical_list: D000596:Amino Acids; D002868:Chromosomal Proteins, Non-Histone; D006570:Heterochromatin; D012097:Repressor Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D000090266:Chromobox Protein Homolog 5; C498700:Suv39h1 protein, mouse; D008780:Methyltransferases; D044763:Ubiquitin-Conjugating Enzymes; D000098843:Ubiquitin-Conjugating Enzyme UBC9