Chromosomal protein HMGN1 modulates histone H3 phosphorylation

Jae Hwan Lim, Frédéric Catez, Yehudit Birger, Katherine L. West, Marta Prymakowska-Bosak, Yuri V. Postnikov*, Michael Bustin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Here we demonstrate that HMGN1, a nuclear protein that binds to nucleosomes and reduces the compaction of the chromatin fiber, modulates histone posttranslational modifications. In Hmgn1-/- cells, loss of HMGN1 elevates the steady-state levels of phospho-S10-H3 and enhances the rate of stress-induced phosphorylation of S10-H3. In vitro, HMGN1 reduces the rate of phospho-S10-H3 by hindering the ability of kinases to modify nucleosomal, but not free, H3. During anisomycin treatment, the phosphorylation of HMGN1 precedes that of H3 and leads to a transient weakening of the binding of HMGN1 to chromatin. We propose that the reduced binding of HMGN1 to nucleosomes, or the absence of the protein, improves access of anisomysin-induced kinases to H3. Thus, the levels of posttranslational modifications in chromatin are modulated by nucleosome binding proteins that alter the ability of enzymatic complexes to access and modify their nucleosomal targets.

Original languageEnglish
Pages (from-to)573-584
Number of pages12
JournalMolecular Cell
Volume15
Issue number4
DOIs
StatePublished - 27 Aug 2004
Externally publishedYes

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