PuSH - Publication Server of Helmholtz Zentrum München

Hergeth, S.P.* ; Dundr, M.* ; Tropberger, P.* ; Zee, B.M.* ; Garcia, B.A.* ; Daujat, S.* ; Schneider, R.*

Isoform-specific phosphorylation of human linker histone H1.4 in mitosis by the kinase Aurora B.

J. Cell Sci. 124, 1623-1628 (2011)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
ISSN (print) / ISBN 0021-9533
e-ISSN 1477-9137
Quellenangaben Volume: 124, Issue: , Pages: 1623-1628 Article Number: , Supplement: ,
Publisher Company of Biologists
Publishing Place Cambridge
Non-patent literature Publications
Reviewing status Peer reviewed