Look at this 🙂 #CryoEM

Structural basis for CTCF-mediated chromatin organization by @lucas.farnunglab.com @voslab.org

www.biorxiv.org/content/10.6...

Exciting work from @lucas.farnunglab.com & @voslab.org report structures of CTCF-nucleosome complexes, revealing that CTCF dimers promote oligomerization of nucleosomes into defined higher-order assemblies involving specific histone-histone and CTCF-CTCF interactions. www.biorxiv.org/content/10.6...

Happy to share part of my postdoctoral work at the @lucas.farnunglab.com lab. Great collaboration with @voslab.org and @andersshansen.bsky.social. “Structural basis for CTCF-mediated chromatin organization” www.biorxiv.org/content/10.6...

It was an honor to participate in this event. I had the opportunity to present my postdoctoral work and interact with the exceptional scientific community at the Helmholtz Munich.

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Early-career researchers: want to run your own lab? 🌟Max Planck Research Groups offer 6+ years, up to €2.7M in funding, open-topic freedom, team support & tenure-track opportunities. Intrigued? 😃Apply by Oct 14, 2025! www.mpg.de/max-planck-r...

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation - Nature Communications ParABS systems partition chromosomal DNA and low-copy plasmids in bacteria. Here, the authors elucidate the mode of interaction between ParA and ParB and clarify how ParB stimulates the ATPase activity of ParA to drive the segregation process.

The final version of our ParA-ParB paper is online.
Thanks to the reviewers for their input and to all the authors for their hard work.

www.nature.com/articles/s41...

The Farnung Lab celebrates Martin Filipovski's thesis defense.

Martin Filipovski successfully defended his PhD thesis today! Congrats, Dr. Filipovski.

I can only recommend @thanbichlerlab.bsky.social as a mentor. You’ll do great science in a friendly environment with great colleagues and live in beautiful Marburg. Apply now!

Thank you Anthony! I hope you enjoy the reading ;)

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-for...

Interested in the bacterial ParABS DNA segregation system? Then have a look at our latest preprint... 🧬

Thanks to the Hennig and Bange groups for the great collaboration!

doi.org/10.1101/2025...

We explored the role of the conserved arginine residue in the ParA-interacting motif of ParB and propose that rather than acting as an arginine finger, it interacts with negatively changed residues on ParA, likely promoting structural changes at its catalytic center required for ATP hydrolysis

We used Hydrogen/deuterium exchange mass spectrometry to show that ParB and nsDNA bind cooperatively to ParA and act synergistically to induce conformational changes in the catalytic site of ParA that correlate with the activation of its ATPase activity.

Moreover, we show that ParB clamps preferentially interact with ParA in their closed CTP-bound conformation ensuring that only partition complex-associated ParB molecules can effectively interact with nucleoid-bound ParA dimers.

We used an integrative structural approach combining AF modeling, X-ray crystallography, and NMR spectroscopy to map the interaction interfaces on both proteins. We found that the N-terminal ParA-binding motif of ParB binds at the ParA dimer interface, near its catalytic center.

I’m very happy to share our latest work on the ParABS system. We investigated the dynamic interaction between the ATPase ParA and the CTPase ParB mediating chromosome segregation in Myxococcus xanthus. I would like to thank all the people involved.