Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-03

AUTHORS

Monika Lachner, Dónal O'Carroll, Stephen Rea, Karl Mechtler, Thomas Jenuwein

ABSTRACT

Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism1,2 that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of similar importance to restrict inappropriate gene expression3,4 if cellular and developmental programmes are to proceed unperturbed. Here we show that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases)5 generate a binding site for HP1 proteins—a family of heterochromatic adaptor molecules6,7 implicated in both gene silencing and supra-nucleosomal chromatin structure. High-affinity in vitro recognition of a methylated histone H3 peptide by HP1 requires a functional chromo domain; thus, the HP1 chromo domain is a specific interaction motif for the methyl epitope on lysine 9 of histone H3. In vivo, heterochromatin association of HP1 proteins is lost in Suv39h double-null primary mouse fibroblasts but is restored after the re-introduction of a catalytically active SUV39H1 HMTase. Our data define a molecular mechanism through which the SUV39H–HP1 methylation system can contribute to the propagation of heterochromatic subdomains in native chromatin. More... »

PAGES

116-120

Journal

TITLE

Nature

ISSUE

6824

VOLUME

410

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/35065132

DOI

http://dx.doi.org/10.1038/35065132

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020526163

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11242053


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