Methylation of K 9 in histone H 3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP 1 β with the nucleosome
نویسندگان
چکیده
Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Am Fassberg 11, 37077 Germany Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Am Fassberg 11, 37077, Germany Biaffin GmbH & Co KG, Heinrich-Plett Strasse 40, 34132 Kassel, Germany Biomolecular Spectroscopy and Single-Molecule Detection, Max Planck Institute for Biophysical Chemistry, Göttingen, Am Fassberg 11, 37077 Germany Protein Chemistry, Leibniz-Institut für molekulare Pharmakologie, Robert-Rössle-Str. 10, 13125 Berlin, Germany Department for Biophysical Chemistry, Technische Universität Braunschweig, Hans-Sommerstr. 10, 38106 Braunschweig, Germany *Correspondence: [email protected] +49 551 201-1340; [email protected] +49 551 201-2220 These authors contributed equally to this work. Current Address: Oxford Nanopore Technologies LTD, Oxford, United Kingdom (SS); Proteros biostructures GmbH, Martinsried, Germany (AS) German Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany
منابع مشابه
Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1β with the nucleosome.
Binding of heterochromatin protein 1 (HP1) to the histone H3 lysine 9 trimethylation (H3K9me3) mark is a hallmark of establishment and maintenance of heterochromatin. Although genetic and cell biological aspects have been elucidated, the molecular details of HP1 binding to H3K9me3 nucleosomes are unknown. Using a combination of NMR spectroscopy and biophysical measurements on fully defined reco...
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