🧩 Also highly relevant: a modeling study from Bin Zhang group predicts condensed euchromatin domains with active protrusions. Perfectly complementary to our findings! 3
www.biorxiv.org/content/10.1...

We thank all the coauthors: @katsuminami.bsky.social‬, Tamura-san, Ashwin-san, Higashi-san, Nishiyama-san, Kanemaki-san, Sasai-san @lschermelleh.bsky.social‬, Toyoda-san. 🙏Special thanks to @healthcare.nikon.com‬ for 3D-SIM support. Also see our related paper‪@TICB bit.ly/4fW4cfL 2

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/...

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 review paper is out@JMB!🧬
@katsuminami.bsky.social‬ @semeigazin.bsky.social‬ ‪@kakonakazato.bsky.social‬ discuss DNA accessibility in euchromatin and heterochromatin of live cells.
Free access: authors.elsevier.com/a/1lHgb54HFZ...
Also check our previous work: www.science.org/doi/10.1126/...

📢 NIG Postdoc Fellowship Call!
www.nig.ac.jp/nig/career-d...
🧬We’re seeking motivated postdocs to join our lab. 🔬We study chromatin behavior in living cells using advanced live-cell imaging and quantitative analysis:
www.science.org/doi/10.1126/...
doi.org/10.2183/pjab...
Interested? Please apply!

🎥 Video: See chromatin in action — each dot is a single nucleosome, dynamically fluctuating in a living HeLa cell (TMR-labeled, 50 ms/frame).
🔬 Original paper: www.science.org/doi/full/10....

🧬My retrospective chromatin review is out @Proc Jpn Acad:
doi.org/10.2183/pjab...
The textbook view of #chromatin as 30-nm fibers is fading.
A new paradigm: chromatin forms #liquid-like domains—locally dynamic, yet globally stable at the chromosome level (viscoelastic)—supporting genome function. ✨

(2/2) Deepest thanks to Maeshima-sensei (@kazu-maeshima.bsky.social), all the collaborators of this paper, and Maeshima-Lab members. Proud to have been involved in this wonderful work!

(1/2) Glad to inform that our work is finally out from Science Advances!
Our Repli-Histo labeling revealed the distinct physical properties of euchromatin (liquid-like) and heterochromatin (gel-like) and their implications for replication timing.

We quantitatively measured nucleosome motion across the 4 chromatin classes, from euchromatin to heterochromatin.
🧪 More euchromatic regions (i.e., earlier-replicated regions) show greater nucleosome motion.
🎉 Congrats @katsuminami.bsky.social @kakonakazato.bsky.social and all collaborators!
2/2

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

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/

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...

Nature research paper: Mechanism for local attenuation of DNA replication at double-strand breaks

https://go.nature.com/4k8AdCX

Hello, world!
(X: katsu_s_minami)