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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.
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Submitted on : Friday, April 19, 2013 - 10:36:26 AM
Last modification on : Tuesday, November 16, 2021 - 5:25:38 AM


  • HAL Id : ensl-00815661, version 1


Claire Falandry, Geneviève Fourel, Vincent Galy, Tutik Ristriani, Béatrice Horard, et al.. CLLD8/KMT1F Is a Lysine Methyltransferase That Is Important for Chromosome Segregation. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285, pp.20234-20241. ⟨ensl-00815661⟩



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