New publication about dynamic interactions of the nucleosome

Impact of histone methylation on the dynamic interaction between heterochromatin proteins and the nucleosome

In a collaboration between Biaffin and the Max Planck Institute for Biophysical Chemistry (Research groups of NMR-based Structural Biology and Chromatin Biochemistry) the impact of histone methylation on the dynamic interaction between heterochromatin proteins and the nucleosome has been investigated and results have been published recently in the renowned Journal of Biological Chemistry. The two research groups of Markus Zweckstetter and Wolfgang Fischle and scientists of Biaffin used a combination of NMR spectroscopy and biophysical measurements (surface plasmon resonance, SPR) to demonstrate that trimethylation of lysine 9 of histone H3 (H3K9me3) works as an on/off switch regulating distinct binding modes of hHP1β to the nucleosome. The results report the first detailed structural analysis of a dynamic protein-nucleosome complex directed by a histone modification and provide a conceptual framework for understanding similar interactions in the context of chromatin. Please read more about this publication in the international Journal of Biological Chemistry:

www.ncbi.nlm.nih.gov/pubmed/22815475 (PubMed)