Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin

Nikhil Raghuram, Hilmar Strickfaden, Darin McDonald, Kylie Williams, He Fang, Craig Mizzen, Jeffrey J. Hayes, John Th'ng, Michael J. Hendzel

Research output: Contribution to journalArticle

Abstract

Histone H1 plays a crucial role in stabilizing higher order chromatin structure. Transcriptionalactivation, DNA replication, and chromosome condensation all require changes in chromatin structure and are correlated with the phosphorylation of histone H1. In this study, we describe a novel interaction between Pin1, a phosphorylation-specific prolyl isomerase, and phosphorylated histone H1. A sub-stoichiometric amount of Pin1 stimulated the dephosphorylation of H1 in vitro and modulated the structure of the C-terminal domain of H1 in a phosphorylation-dependent manner. Depletion of Pin1 destabilized H1 binding to chromatin only when Pin1 binding sites on H1 were present. Pin1 recruitment and localized histone H1 phosphorylation were associated with transcriptional activation independent of RNA polymerase II. We thus identify a novel form of histone H1 regulation through phosphorylation-dependent proline isomerization, which has consequences on overall H1 phosphorylation levels and the stability of H1 binding to chromatin.

Original languageEnglish (US)
Pages (from-to)57-71
Number of pages15
JournalJournal of Cell Biology
Volume203
Issue number1
DOIs
StatePublished - 2013

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin'. Together they form a unique fingerprint.

  • Cite this

    Raghuram, N., Strickfaden, H., McDonald, D., Williams, K., Fang, H., Mizzen, C., Hayes, J. J., Th'ng, J., & Hendzel, M. J. (2013). Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin. Journal of Cell Biology, 203(1), 57-71. https://doi.org/10.1083/jcb.201305159