Masa A. Shimazoe
Ph. D. Student in Maeshima lab in NIG @kazu-maeshima.bsky.social
Biophysics, Chromatin / Kyoto Uni. → NIG
- Reposted by Masa A. ShimazoeMy PhD students Aoi Otsuka @masaashimazoe.bsky.social et al. published @csf-jscb.bsky.social 🎉 Single-nucleosome imaging in an oncogene-inducible human carcinogenesis model shows biphasic chromatin dynamics (1–3 d same; 5–7 d ↑; back by week 4). Congrats! 👉 doi.org/10.1247/csf....
- Reposted by Masa A. ShimazoeExcited to share our latest fully in-house paper! 🎉 We show how cohesin integrates loop extrusion with sister tethering to guide the homology search during DNA repair. Huge congratulations to all authors, and to @fedeteloni.bsky.social for leading this work 👏 We’re excited to see his next steps!
- I am happy to share that my postdoctoral work in the @gerlichlab.bsky.social at @imbavienna.bsky.social is finally out 🎉! Our study reveals how cohesin guides focused and accurate homology search. Read more 👉 www.science.org/doi/10.1126/... Follow along for key insights and updates! 🧵
- Reposted by Masa A. ShimazoeI am happy to share that my postdoctoral work in the @gerlichlab.bsky.social at @imbavienna.bsky.social is finally out 🎉! Our study reveals how cohesin guides focused and accurate homology search. Read more 👉 www.science.org/doi/10.1126/... Follow along for key insights and updates! 🧵
- Reposted by Masa A. ShimazoeOur Science paper is out! Huge congratulations to @huabin-zhou.bsky.social, Mike Rosen, and the brilliant @janhuemar.bsky.social @juliamaristany.bsky.social and @kieran-russell.bsky.social from our group News: bit.ly/4avnkAr and bit.ly/3XBGVHS Great perspective by @vram142.bsky.social +K Zhang
- @science.org 🧬🔬 Multiscale structure of #chromatin condensates explains phase separation and material properties | Science www.science.org/doi/10.1126/... @janhuemar.bsky.social et al.
- Reposted by Masa A. ShimazoeA new, nerdy paper. We figured out (some) of the rules underlying cell-permeability of probes and designed ligands that light up, grab, and move proteins around. Awesome @hhmijanelia.bsky.social x @uwmadison.bsky.social x @stjuderesearch.bsky.social collaboration! www.pnas.org/doi/10.1073/...
- Reposted by Masa A. ShimazoeCheck out our new work, led by talented @janhuemar.bsky.social, where we uncover that pioneer factor Oct4 remodels chromatin for DNA access not by opening it but by exploiting nucleosome breathing and forming clusters 🔥🔥🔥
- 🚨 🚨 🚨 New preprint alert!!! 🚨 🚨 🚨 In the past, we have learnt that Oct4 can induce nucleosome breathing on the mono-nucleosome level. But what happens when you have a fibre of multiple nucleosomes? www.biorxiv.org/content/10.1... @rcollepardo.bsky.social @juliamaristany.bsky.social
- Reposted by Masa A. Shimazoe🚨 🚨 🚨 New preprint alert!!! 🚨 🚨 🚨 In the past, we have learnt that Oct4 can induce nucleosome breathing on the mono-nucleosome level. But what happens when you have a fibre of multiple nucleosomes? www.biorxiv.org/content/10.1... @rcollepardo.bsky.social @juliamaristany.bsky.social
- Reposted by Masa A. ShimazoeThis 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. scim.ag/4mTE1Z6
- Reposted by Masa A. ShimazoeThis year’s #NobelPrize in Physiology or Medicine has been awarded to three scientists for discovering how the immune system distinguishes friend from foe. scim.ag/3Wt5rdi
- Reposted by Masa A. Shimazoe@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
- 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)
- 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/...
- Condensed chromatin domain structure and cohesin-constrained mobility assure independent transcription regulation for each domain! Also consistent with many previous studies. (4/n)
- Reposted by Masa A. ShimazoeIs 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. ShimazoeOne 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)
- Reposted by Masa A. ShimazoePleased 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!
- 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
- Go to the link to see our preprint about linker histone H1! www.biorxiv.org/content/10.1...
- 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.
- Reposted by Masa A. Shimazoe🔬 #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. ShimazoeOur 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. ShimazoeOur 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)
- 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)
- 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)
- 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)
- Reposted by Masa A. ShimazoeExcited 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!
- 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/
- Reposted by Masa A. ShimazoeUsing 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
- Reposted by Masa A. ShimazoeOur 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/
- Reposted by Masa A. ShimazoeIn 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 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/
- Reposted by Masa A. ShimazoeOur 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...
