English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons36513

Stützer,  A.
Research Group of Chromatin Biochemistry, MPI for biochemical chemistry, Max Planck Society;

/persons/resource/persons188389

Kiesel,  A.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons128572

Söding,  J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15074

Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for biochemical chemistry, Max Planck Society;

Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

2243234-Suppl.pdf
(Supplementary material), 7MB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0029-6468-4
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.