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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilungsunabhängige Arbeitsgruppen     Display Documents



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ID: 733151.0, MPI für Entwicklungsbiologie / Abteilungsunabhängige Arbeitsgruppen
Modulations of DNA Contacts by Linker Histones and Post-translational Modifications Determine the Mobility and Modifiability of Nucleosomal H3 Tails
Authors:Stutzer, A.; Liokatis, S.; Kiesel, A.; Schwarzer, D.; Sprangers, R.; Soding, J.; Selenko, P.; Fischle, W.
Date of Publication (YYYY-MM-DD):2016-01-21
Title of Journal:Mol Cell
Volume:61
Issue / Number:2
Start Page:247
End Page:259
Review Status:Internal review
Audience:Not Specified
Abstract / Description: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.
Free Keywords:Acetylation; Amino Acid Sequence; Animals; DNA/*metabolism; Genome; Histones/chemistry/*metabolism; Molecular Sequence Data; Nucleosomes/*metabolism; Phosphorylation; Protein Binding; *Protein Processing, Post-Translational; Xenopus laevis
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilungsunabhängige Arbeitsgruppen/Arbeitsgruppe Sprangers
MPI für biophysikalische Chemie
External Affiliations:Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rossle Strasse 10, 13125 Berlin, Germany. Research Group of Computational Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany. Department of Chemical Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rossle Strasse 10, 13125 Berlin, Germany. Max Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tubingen, Germany. Research Group of Computational Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany; Gene Center and Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universitat Munchen, Feodor-Lynen-Strasse 25, 81377 Munich, Germany. Department of NMR-Supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rossle Strasse 10, 13125 Berlin, Germany. Electronic address: selenko@fmp-berlin.de. Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany. Electronic address: wfischl@mpibpc.mpg.de.
Identifiers:ISSN:1097-4164 (Electronic) 1097-2765 (Linking) %R 10.1... [ID No:1]
URL:https://www.ncbi.nlm.nih.gov/pubmed/26778125 [ID No:2]
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