Masa A. Shimazoe
@masaashimazoe.bsky.social
110 followers 90 following 15 posts
Ph. D. Student in Maeshima lab in NIG @kazu-maeshima.bsky.social Biophysics, Chromatin / Kyoto Uni. → NIG
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Reposted by Masa A. Shimazoe
science.org
This year’s #NobelPrize in Chemistry has gone to the architects of molecular “cages” that could be used for everything from carbon capture to drug delivery. https://scim.ag/4mTE1Z6
Architects of molecular cages win Chemistry Nobel
Susumu Kitagawa, Richard Robson, and Omar Yaghi honored for developing metal-organic frameworks
Reposted by Masa A. Shimazoe
Reposted by Masa A. Shimazoe
janeskok.bsky.social
@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
masaashimazoe.bsky.social
Condensed chromatin domain structure and cohesin-constrained mobility assure independent transcription regulation for each domain!
Also consistent with many previous studies.
(4/n)
masaashimazoe.bsky.social
We got a clue to my unsolved question from high school 🌱
“Chromatin loop organization insulates transcription”—a schematic I once scribbled in my textbook like this.
But ever since, I’ve wondered: How can neighboring loops avoid interacting?
(3/n)
Reposted by Masa A. Shimazoe
kazu-maeshima.bsky.social
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/...
Reposted by Masa A. Shimazoe
shiori-iida.bsky.social
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)
masaashimazoe.bsky.social
All efforts by coauthors made this happen! :
@katsuminami.bsky.social, Tamura-san, Ashwin-san, Higashi-san, Nishiyama-san, Kanemaki-san, Sasai-san, @lschermelleh.bsky.social ‬, Toyoda-san, Kurokawa-san.
And, as always, I deeply appreciate @kazu-maeshima.bsky.social 's supervision!
(2/n)
masaashimazoe.bsky.social
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)
kazu-maeshima.bsky.social
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/...
masaashimazoe.bsky.social
Thank you very much!
Hope you enjoy reading!
masaashimazoe.bsky.social
Thank you for your kind words.
It was great to meet you, and I enjoyed your talk!
masaashimazoe.bsky.social
And again, Fantastic meeting! 🔬
Single-molecule studies are advancing biology into new territory—thrilled to be involved. 💡
#EMBLSingleMolecule
masaashimazoe.bsky.social
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.
masaashimazoe.bsky.social
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
Reposted by Masa A. Shimazoe
events.embl.org
🔬 #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!
Reposted by Masa A. Shimazoe
kazu-maeshima.bsky.social
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
Reposted by Masa A. Shimazoe
kazu-maeshima.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
Reposted by Masa A. Shimazoe
masaashimazoe.bsky.social
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)
masaashimazoe.bsky.social
Huge thanks to Rosana @rcollepardo.bsky.social, Charlie, Jan @janhuemar.bsky.social, and Stephen! 🙌
Their simulations revealed in stunning detail how H1 and nucleosomes interact.
I was amazed—so consistent with our experiments! 🔬💻
(4/n)
masaashimazoe.bsky.social
Single molecule imaging revealed that H1 behaves like a liquid inside chromatin! 🫧
It's amazing to witness how H1 behaves in living cells 🔬✨
(3/n)
masaashimazoe.bsky.social
H1 is the most abundant chromatin protein, condensing chromatin—but how? 🤔
The textbook model suggests H1 stabilizes 30-nm fiber, but recent studies dispute this. So, what's the true mechanism?
We think: H1 acts as a liquid-like "glue"! (2/n)
masaashimazoe.bsky.social
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)
Reposted by Masa A. Shimazoe
janhuemar.bsky.social
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!
kazu-maeshima.bsky.social
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/