@kazu_maeshima from the Genome Dynamics Laboratory at the National Institute of Genetics (@NIG_idenken) will present groundbreaking research on chromatin organization and behavior in live cells revealed by super-resolution imaging. nyulangone.zoom.us/webinar/regi... #chromatin2025

Is euchromatin really “open”? Our new study @bioRxiv suggests otherwise. Using super-resolution imaging @shiori-iida.bsky.social‬ @masaashimazoe.bsky.social reveals: Euchromatin forms condensed domains in live cells. Cohesin constrains them and prevents domain mixing. www.biorxiv.org/cgi/content/...

One more movie! Using the RL algorithm (from pnas.org/doi/10.1073/...), @masaashimazoe.bsky.social analyzed our nucleosome tracking data and classified them by their mobility. Hotter color = faster motion (Slow🔵→ 🟢 → 🟡 → 🟠 Fast)

Euchromatin is mostly condensed⁉️ With @shiori-iida.bsky.social , We revealed the detailed structure of euchromatin using super-resolution imaging. Cohesin regulates the function of euchromatin via chromatin dynamics! (1/n)

Pleased to see this study out, combining experimental work from our lab at the @cbitoulouse.bsky.social, in particular by @nathaliebastie.bsky.social and @beckof.bsky.social, and from Laura Chaptal and @alengronne.bsky.social at IGH Montpellier @cnrs.fr @cnrsbiologie.bsky.social Congrats to all!

And again, Fantastic meeting! 🔬 Single-molecule studies are advancing biology into new territory—thrilled to be involved. 💡 #EMBLSingleMolecule

I had an amazing time at EMBL Heidelberg! I was absolutely impressed by the facilities—everything operates on a completely different scale here. Definitely hope to work in an environment like this someday.

Honored to receive 1st Place Poster Award 🏆 at the EMBL meeting "Gene Regulation: One Molecule at a Time"! Thank you to all who visited and engaged in exciting discussions. Grateful to the organizers for an excellent event! #EMBLSingleMolecule

🔬 #EMBLSingleMolecule poster session highlights 📜 Big ideas, bold questions, and lots of sticky notes! From molecular mechanics to late-breaking results – the poster session was buzzing with energy and conversation 💬 Loved seeing early-career researchers shine!

Our new preprint 🧬🔗 www.biorxiv.org/content/10.1... BRD4-NUT forms liquid-like condensates that locally constrain nucleosomes via BRD4-mediated crosslinking— physical control of #chromatin by #LLPS transcription condensates. @semeigazin.bsky.social @katsuminami.bsky.social @masaashimazoe.bsky.social

Our new paper is out@ScienceAdvances👇 www.science.org/doi/10.1126/... 🧬Our Repli-Histo labeling marks nucleosomes in euchromatin and heterochromatin in live human cells. 🔍 @katsuminami.bsky.social et al. have developed a chromatin behavior atlas within the nucleus. 1/2

My first, first author paper is now on bioRxiv! 🤩 Linker histone H1 is a liquid-like "glue" condensing chromatin, which revises textbooks! 📖✨ biorxiv.org/content/10.1... Huge thanks to my PI, @kazu-maeshima.bsky.social, for supervision. Amazing collab with @rcollepardo.bsky.social’s group!" (1/n)

My first, first author paper is now on bioRxiv! 🤩 Linker histone H1 is a liquid-like "glue" condensing chromatin, which revises textbooks! 📖✨ biorxiv.org/content/10.1... Huge thanks to my PI, @kazu-maeshima.bsky.social, for supervision. Amazing collab with @rcollepardo.bsky.social’s group!" (1/n)

Excited to share our newest collaboration with @kazu-maeshima.bsky.social and @masaashimazoe.bsky.social, where we show that H1 acts as a liquid-like glue in chromatin. Go check the paper on the biorXiv!

Using single-H1 imaging and computational modeling, we show that most H1 behaves like a liquid inside chromatin domains rather than binding stably to nucleosomes as in the textbook model. Congrats @masaashimazoe.bsky.social & all contributors! 🎉 2/ 🔗 bit.ly/4h7S3Dn

Our new preprint is out＠bioRxiv: www.biorxiv.org/content/10.1... @masaashimazoe.bsky.social et al. reveal that linker histone H1 acts as a liquid-like glue to organize chromatin in living cells. 🎉 Fantastic collab with @rcollepardo.bsky.social @janhuemar.bsky.social and others—huge thanks! 🙌 1/

In this wonderful collaboration with K Maeshima and M Shimazoe we show that H1 in living cells acts as a liquid-like glue not a driver of stiff zigzag fibers 🔥🔥🔥 Each H1 bridges multiple nucleosomes and exchanges nucleosomes frequently: boosting both compaction and dynamical behaviour of chromatin

Our new review on how the #chromatin domain is formed in the cell is now available @Curr Opin Struct Biol.📄✨ We critically discuss the domain formation mechanism from a physical perspective, including #phase-separation and #condensation. 📥 Free-download link: authors.elsevier.com/a/1keGn,LqAr...

This is my new account on Bluesky !!!