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

ABSTRACT: 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 responses. Here, we report that lysine (Lys) 79 of histone H3, which resides in the globular domain, is methylated in eukaryotic organisms. In the yeast Saccharomyces cerevisiae, Lys 79 of histone H3 is methylated by Dot1, a protein shown previously to play a role in telomeric silencing. Mutations of Lys 79 of histone H3 and mutations that abolish the catalytic activity of Dot1 impa

SUBMITTER: Ng HH 

PROVIDER: S-EPMC186335 | biostudies-literature | 2002 Jun

REPOSITORIES: biostudies-literature