title: CLLD8/KMT1F is a lysine methyltransferase that is important for chromosome segregation.
abstract: Proteins bearing a SET domain have been shown to methylate lysine residues in histones and contribute to chromatin architecture. Methylation of histone H3 at lysine 9 (H3K9) has emerged as an important player in the formation of heterochromatin, chromatin condensation, and transcriptional repression. Here, we have characterized a previously undescribed member of the histone H3K9 methyltransferase family named CLLD8 (or SETDB2 or KMT1F). This protein contributes to the trimethylation of both interspersed repetitive elements and centromere-associated repeats and participates in the recruitment of heterochromatin protein 1 to centromeres. Consistently, depletion in CLLD8/KMT1F coincides with a loss of CENP proteins and delayed mitosis, suggesting that this protein participates in chromosome condensation and segregation. Altogether, our results provide evidence that CLLD8/KMT1F is recruited to heterochromatin regions and contributes in vivo to the deposition of trimethyl marks in concert with SUV39H1/KMT1A.
authors.affiliation: Laboratoire de Biologie Moléculaire de la Cellule, CNRS Unité Mixte de Recherche (UMR) 5239, Ecole Normale Supérieure de Lyon (ENS) Lyon, Université Claude Bernard Lyon 1 (UCBL1), Institut Fédératìf de Recherche (IFR)128, Faculté de Médecine Lyon Sud, F-69600 Oullins, France.
authors.forename: Claire
authors.initials: C
authors.lastname: Falandry
authors.forename: Geneviève
authors.initials: G
authors.lastname: Fourel
authors.forename: Vincent
authors.initials: V
authors.lastname: Galy
authors.forename: Tutik
authors.initials: T
authors.lastname: Ristriani
authors.forename: Béatrice
authors.initials: B
authors.lastname: Horard
authors.forename: Elsa
authors.initials: E
authors.lastname: Bensimon
authors.forename: Gilles
authors.initials: G
authors.lastname: Salles
authors.forename: Eric
authors.initials: E
authors.lastname: Gilson
authors.forename: Frédérique
authors.initials: F
authors.lastname: Magdinier
mesh_terms: D001665:Binding Sites; D015153:Blotting, Western; D002460:Cell Line; D020090:Chromosome Segregation; D005455:Fluorescent Antibody Technique; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006367:HeLa Cells; D006570:Heterochromatin / Q000378:metabolism; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007211:Indoles / Q000737:chemistry; D008745:Methylation; D008780:Methyltransferases / Q000235:genetics / Q000378:metabolism; D018613:Microscopy, Confocal; D008938:Mitosis; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D006570:Heterochromatin; D006657:Histones; D007211:Indoles; D009687:Nuclear Proteins; D012097:Repressor Proteins; D049452:Green Fluorescent Proteins; C007293:DAPI; C407843:SUV39H1 protein, human; D008780:Methyltransferases; D011495:Histone-Lysine N-Methyltransferase
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