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  A cascade of histone modifications induces chromatin condensation in mitosis.

Wilkins, B. J., Rall, N. A., Ostwal, Y., Kruitwagen, T., Hiragami-Hamada, K., Winkler, M., et al. (2014). A cascade of histone modifications induces chromatin condensation in mitosis. Science, 343(6166), 77-80. doi:10.1126/science.1244508.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-11C0-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-BBF2-B
Genre: Journal Article

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 Creators:
Wilkins, B. J., Author
Rall, N. A., Author
Ostwal, Y., Author
Kruitwagen, T., Author
Hiragami-Hamada, K., Author
Winkler, M., Author
Barral, Y., Author
Fischle, W.1, Author              
Neumann, H., Author
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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 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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Language(s): eng - English
 Dates: 2014-01-03
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/science.1244508
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 343 (6166) Sequence Number: - Start / End Page: 77 - 80 Identifier: -