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

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 recogni...

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Bibliografiske detaljer
Main Authors: Ng, Huck Hui, Feng, Qin, Wang, Hengbin, Erdjument-Bromage, Hediye, Tempst, Paul, Zhang, Yi, Struhl, Kevin
Format: Artigo
Sprog:Inglês
Udgivet: Cold Spring Harbor Laboratory Press 2002
Fag:
Research Paper
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC186335/
https://ncbi.nlm.nih.gov/pubmed/12080090
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.1001502
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