LCBM

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

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/...

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

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...

Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes Single-molecule experiments show that active conformation formation controls chromatin ubiquitylation kinetics by variant PRC1.

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