Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain.

By Qin Feng, Hengbin Wang, Huck-Hui Ng, H. Erdjument‐Bromage, Paul Tempst, Kevin Struhl, Yi Zhang. Current Biology, 2002

866 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6825dda690cb6a7f463366fc0df1c94a1bbbfcf3

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Citations in the corpus

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks (2004, background): “The enzyme that methylates Lys 79 in human cells is DOT1L, an evolutionarily conserved methyltransferas”
The diverse functions of histone lysine methylation (2005, background): “With regard to H3-K79 methylation, the responsible enzymes are Dot1 or its homologues, which are the only lysine methyltransferases that have been identified so far that lack an identifiable SET domain 107–110 .”
hDOT1L links histone methylation to leukemogenesis. (2005, neutral): “AF10 and hDOT1L that were fused to the VP16 ac-yeast DOT1 and demonstrated its H3-K79-specific tivation domain and the Gal4-DNA binding domain, methyltransferase activity (Feng et al., 2002).”
The SET-domain protein superfamily: protein lysine methyltransferases (2005, background): “The exception to the rule is the DOT1 family, members of which methylate K79 in the globular region of histone H3 and which are structurally not related to SET-domain proteins [4-6].”
Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “Recently, Bian et al. found that tumor cells can absorb a large amount of methionine through the methionine transporter SLC43A2, and competition results in methionine deficiency in T cells, thus affecting epigenetic changes, including loss of H3K79me2 in T cells and impairing the effector function o”
Selective Killing of Mixed Lineage Leukemia Cells by a Potent Small-Molecule DOT1L Inhibitor (2011, neutral): “DOT1L catalyzes themethylation of H3K79, a chromatinmodification associated with actively transcribed genes (Feng et al., 2002; Steger et al., 2008).”
Genome-wide map of nucleosome acetylation and methylation in yeast. (2005, neutral): “Histone H3K79me3, which is atalyzed by Dot1 (Feng et al., 2002; Ng et al., 2003a; an Leeuwen et al., 2002), is enriched within genes, but, nlike the other modifications studied here, this enrichent is not clearly associated with active transcription Figure 4F).”
Potent inhibition of DOT1L as treatment of MLL-fusion leukemia. (2013, background): “DOT1L is a histone methyltransferase enzyme that targets lysine 79 in the globular domain of histone H3 (H3K79) for mono-, di-, or trimethylation (H3K79me1, me2, or me3).(19,20) As a result, MLLfusion proteins gain the ability to recruit DOT1L to MLL target genes where the resulting hypermethylation”
An epigenetic road map for histone lysine methylation (2003, background): “Research Institute of Molecular Pathology (IMP), The Vienna Biocenter, Dr Bohrgasse7, A-1030 Vienna, Austria *Author for correspondence (e-mail: jenuwein@nt.imp.univie.ac.at) This poster is dedicated to the memory of Alan Wolffe, an inspirational and integrative leader for the field of chromatin reg”