Our new study of chromatin ubiquitylation by variant PRC1 on the single-molecule scale: We visualize directly how vPRC1 ubiquitylates neighboring nucleosomes during a single binding event, showing a potential mechanism how H2Aub domains are established. www.science.org/doi/10.1126/...

If you always wanted to know the kinetics of how the Polycomb enzymes modify chromatin, we are thrilled to share our work!!! 🎉📄🧬🔬 Thank you, @beatfierz.bsky.social for all the guidance as well as the @lcbm-epfl.bsky.social group members for all the support! doi.org/10.1126/scia...

Check out our new study of chromatin ubiquitylation. @alexateslenko.bsky.social visualized directly at single molecule scale how vPRC1 ubiquitylates neighboring nucleosomes. These results suggest potential mechanism on how H2Aub domains are established. 👇👇👇 www.science.org/doi/10.1126/...

Congratulations @matteodoudin.bsky.social for this PhD fellowship 🥳🎉. Stay tuned for his next achievements about nucleosome depletion.

#SIRT7 is a histone deacetylase with highly specific activity on #chromatin substrates. We just published mechanism-based #cryoEM structures of #SIRT7 on nucleosomes to understand its activity 👇 www.nature.com/articles/s41... (1/8) #ChemBio #ChemSky