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Open Access Green as soon as Postprint is submitted to ZB.
Isoform-specific phosphorylation of human linker histone H1.4 in mitosis by the kinase Aurora B.
J. Cell Sci. 124, 1623-1628 (2011)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
2011
HGF-reported in Year
0
ISSN (print) / ISBN
0021-9533
e-ISSN
1477-9137
Journal
Journal of Cell Science
Quellenangaben
Volume: 124,
Pages: 1623-1628
Publisher
Company of Biologists
Publishing Place
Cambridge
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-502800-001
PubMed ID
21511733
Erfassungsdatum
2011-12-31