Fiche publication
Date publication
mai 2011
Journal
Journal of cell science
Auteurs
Membres identifiés du Cancéropôle Est :
Dr DAUJAT Sylvain
Tous les auteurs :
Hergeth SP, Dundr M, Tropberger P, Zee BM, Garcia BA, Daujat S, Schneider R
Lien Pubmed
Résumé
The linker histone H1 plays an essential role in maintaining and establishing higher-order chromatin structure. As with core histones, histone H1 is also extensively covalently modified. We showed previously that phosphorylation of S27 in human histone H1.4 (H1.4S27-P), prevents binding of heterochromatin protein 1 (HP1) family members (officially known as chromobox protein homologs) to the neighboring dimethylated K26. Here, we present the first functional characterization of H1.4S27-P in vivo and in vitro. We show that H1.4S27 phosphorylation is cell-cycle-regulated and its levels peak on metaphase chromosomes. We identify further Aurora B as the kinase phosphorylating H1.4S27. We demonstrate that histone H1.4 is the only somatic linker histone variant targeted by Aurora B and that Aurora B exclusively phosphorylates S27. Adjacent K26 dimethylation can regulate Aurora B activity towards S27, uncovering a crosstalk between these modifications. Finally, our fluorescence recovery after photobleaching (FRAP) analysis on histone H1.4 mutants suggests a role of S27 phosphorylation in the regulation of histone H1.4 mobility and chromatin binding in mitosis.
Mots clés
Animals, Aurora Kinase B, Aurora Kinases, Chromosomal Proteins, Non-Histone, chemistry, HeLa Cells, Heterochromatin, metabolism, Histones, chemistry, Humans, Methylation, Mice, Mitosis, physiology, NIH 3T3 Cells, Phosphorylation, Protein Isoforms, Protein-Serine-Threonine Kinases, metabolism, Substrate Specificity
Référence
J. Cell. Sci.. 2011 May;124(Pt 10):1623-8
