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Article

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association.

Genes & development - 15 Jun 2002

Ng Huck Hui, Feng Qin, Wang Hengbin, Erdjument-Bromage Hediye, Tempst Paul, Zhang Yi, Struhl Kevin

Abstract excerpt

The amino-terminal histone tails are subject to covalent post-translational modifications such as acetylation, methylation, and phosphorylation. In the histone code hypothesis, these exposed and unstructured histone tails are accessible to a repertoire of regulatory factors that specifically recognize the various modified histones, thereby generating altered chromatin structures that mediate specific biological...

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Identifiers

PMID: 12080090
DOI: 10.1101/gad.1001502
PMCID: PMC186335

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association.PMID 12080090Read ↗

Dot1p modulates silencing in yeast by methylation of the nucleosome core.Semantic proximity Read ↗

The histone H3K79 methyltransferase Dot1L is essential for mammalian development and heterochromatin structure.Semantic proximity Read ↗

Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast.Semantic proximity Read ↗

Multiple histone modifications in euchromatin promote heterochromatin formation by redundant mechanisms in Saccharomyces cerevisiae.Semantic proximity Read ↗

The mechanism of cross-talk between histone H2B ubiquitination and H3 methylation by Dot1LSemantic proximity Read ↗

Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism.Semantic proximity Read ↗

H3K79 methylation and H3K36 tri-methylation synergistically regulate gene expression in pluripotent stem cellsSemantic proximity Read ↗

Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase.Semantic proximity Read ↗

The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation.Semantic proximity Read ↗

Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9.Semantic proximity Read ↗

A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3.Semantic proximity Read ↗

Simultaneous mutation of methylated lysine residues in histone H3 causes enhanced gene silencing, cell cycle defects, and cell lethality in Saccharomyces cerevisiae.Semantic proximity Read ↗

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