Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity.
Nucleic Acids Res
; 47(13): 6726-6736, 2019 07 26.
Article
em En
| MEDLINE
| ID: mdl-31165882
ABSTRACT
Heterochromatin is a distinctive chromatin structure that is essential for chromosome segregation, genome stability and regulation of gene expression. H3K9 methylation (H3K9me), a hallmark of heterochromatin, is deposited by the Su(var)3-9 family of proteins; however, the mechanism by which H3K9 methyltransferases bind and methylate the nucleosome is poorly understood. In this work we determined the interaction of Clr4, the fission yeast H3K9 methyltransferase, with nucleosomes using nuclear magnetic resonance, biochemical and genetic assays. Our study shows that the Clr4 chromodomain binds the H3K9me3 tail and that both, the chromodomain and the disordered region connecting the chromodomain and the SET domain, bind the nucleosome core. We show that interaction of the disordered region with the nucleosome core is independent of H3K9me and contributes to H3K9me in vitro and in vivo. Moreover, we show that those interactions with the nucleosome core are contributing to de novo deposition of H3K9me and to establishment of heterochromatin.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Schizosaccharomyces
/
DNA Fúngico
/
Heterocromatina
/
Nucleossomos
/
Histona-Lisina N-Metiltransferase
/
Proteínas de Ciclo Celular
/
Proteínas de Schizosaccharomyces pombe
/
Código das Histonas
/
Metiltransferases
Idioma:
En
Revista:
Nucleic Acids Res
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Alemanha