A cascade of histone modifications induces chromatin condensation in mitosis

Bryan J. Wilkins; Nils A. Rall; Yogesh Ostwal; Tom Kruitwagen; Kyoko Hiragami-Hamada; Marco Winkler; Yves Barral; Wolfgang Fischle; Heinz Neumann

doi:10.1126/science.1244508

A cascade of histone modifications induces chromatin condensation in mitosis

Bryan J. Wilkins, Nils A. Rall, Yogesh Ostwal, Tom Kruitwagen, Kyoko Hiragami-Hamada, Marco Winkler, Yves Barral, Wolfgang Fischle, Heinz Neumann^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

196 Scopus citations

Abstract

Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.

Original language	English (US)
Pages (from-to)	77-80
Number of pages	4
Journal	SCIENCE
Volume	343
Issue number	6166
DOIs	https://doi.org/10.1126/science.1244508
State	Published - 2014
Externally published	Yes

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title = "A cascade of histone modifications induces chromatin condensation in mitosis",

abstract = "Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.",

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AU - Wilkins, Bryan J.

AU - Rall, Nils A.

AU - Ostwal, Yogesh

AU - Kruitwagen, Tom

AU - Hiragami-Hamada, Kyoko

AU - Winkler, Marco

AU - Barral, Yves

AU - Fischle, Wolfgang

AU - Neumann, Heinz

PY - 2014

Y1 - 2014

N2 - Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.

AB - Metaphase chromosomes are visible hallmarks of mitosis, yet our understanding of their structure and of the forces shaping them is rudimentary. Phosphorylation of histone H3 serine 10 (H3 S10) by Aurora B kinase is a signature event of mitosis, but its function in chromatin condensation is unclear. Using genetically encoded ultraviolet light-inducible cross-linkers, we monitored protein-protein interactions with spatiotemporal resolution in living yeast to identify the molecular details of the pathway downstream of H3 S10 phosphorylation. This modification leads to the recruitment of the histone deacetylase Hst2p that subsequently removes an acetyl group from histone H4 lysine 16, freeing the H4 tail to interact with the surface of neighboring nucleosomes and promoting fiber condensation. This cascade of events provides a condensin-independent driving force of chromatin hypercondensation during mitosis.

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A cascade of histone modifications induces chromatin condensation in mitosis

Abstract

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