1. A cascade of histone modifications induces chromatin condensation in mitosis.
- Author
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Wilkins BJ, Rall NA, Ostwal Y, Kruitwagen T, Hiragami-Hamada K, Winkler M, Barral Y, Fischle W, and Neumann H
- Subjects
- Adenosine Triphosphatases metabolism, Chromosomes, Fungal genetics, Chromosomes, Fungal metabolism, Cross-Linking Reagents chemistry, Cross-Linking Reagents radiation effects, DNA-Binding Proteins metabolism, Lysine metabolism, Multiprotein Complexes metabolism, Phosphorylation, Protein Interaction Mapping, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins metabolism, Sirtuin 2 metabolism, Chromatin metabolism, Histones metabolism, Mitosis, Protein Processing, Post-Translational, Saccharomyces cerevisiae metabolism, Serine metabolism
- 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.
- Published
- 2014
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