A Cascade of Histone Modifications Induces Chromatin Condensation in Mitosis

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Science  03 Jan 2014:
Vol. 343, Issue 6166, pp. 77-80
DOI: 10.1126/science.1244508

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Chromosome Condensation

The forces that shape the structure of the highly condensed metaphase chromosomes seen during cell division in eukaryotes are still largely unknown. In vitro evidence suggests that the amino-terminal tails of the histones—such as interaction of the histone H4 tail with H2A-H2B—play an important role in chromosome hypercondensation. Wilkins et al. (p. 77) used ultraviolet cross-linker amino acids in the histones of bakers' yeast to show that during early mitosis, phosphorylation of H3 threonine 3 by Haspin kinase recruits the chromosome passenger complex (CPC). The subsequent phosphorylation of H3 serine 10 by CPC allows the recruitment of the deacetylase Hst2p to nucleosomes. Hst2p drives the deacetylation of H4 lysine 16, facilitating the interaction between H4 and H2A-H2B in neighboring nucleosomes, promoting chromatin condensation.


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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