Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 26, Pages 20234-20241Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.052399
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Funding
- La Ligue Nationale contre le Cancer (Comite de la Drome and Comite du Rhone)
- l'Association pour la Recherche sur le Cancer (Programme National et Programme Alliance des Recherches sur le Cancer)
- Canceropole Rhone-Alpes
- European Economic Community
- French Minister of Research
- La Fondation pour la Recherche Medicale
- La Ligue Contre le Cancer
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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.
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