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  Modulations of DNA contacts by linker histones and post-translational modifications determine the mobility and modifiability of nucleosomal H3 tails.

Stützer, A., Liokatis, S., Kiesel, A., Schwarzer, D., Sprangers, R., Söding, J., et al. (2016). Modulations of DNA contacts by linker histones and post-translational modifications determine the mobility and modifiability of nucleosomal H3 tails. Molecular Cell, 61(2), 247-259. doi:10.1016/j.molcel.2015.12.015.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-6468-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-203B-1
Genre: Journal Article

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 Creators:
Stützer, A.1, Author              
Liokatis, S., Author
Kiesel, A.2, Author              
Schwarzer, D., Author
Sprangers, R., Author
Söding, J.2, Author              
Selenko, P., Author
Fischle, W.1, Author              
Affiliations:
1Research Group of Chromatin Biochemistry, MPI for biochemical chemistry, Max Planck Society, ou_578604              
2Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1933286              

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 Abstract: Post-translational histone modifications and linker histone incorporation regulate chromatin structure and genome activity. How these systems interface on a molecular level is unclear. Using biochemistry and NMR spectroscopy, we deduced mechanistic insights into the modification behavior of N-terminal histone H3 tails in different nucleosomal contexts. We find that linker histones generally inhibit modifications of different H3 sites and reduce H3 tail dynamics in nucleosomes. These effects are caused by modulations of electrostatic interactions of H3 tails with linker DNA and largely depend on the C-terminal domains of linker histones. In agreement, linker histone occupancy and H3 tail modifications segregate on a genome-wide level. Charge-modulating modifications such as phosphorylation and acetylation weaken transient H3 tail-linker DNA interactions, increase H3 tail dynamics, and, concomitantly, enhance general modifiability. We propose that alterations of H3 tail-linker DNA interactions by linker histones and charge-modulating modifications execute basal control mechanisms of chromatin function.

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Language(s): eng - English
 Dates: 2016-01-142016-01-21
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2015.12.015
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 61 (2) Sequence Number: - Start / End Page: 247 - 259 Identifier: -