
Kurumizaka Lab
@KurumizakaLab
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The University of Tokyo / Chromatin / nucleosome/epigenetics/The singing structural biologist
The University of Tokyo
Joined October 2018
Our new paper has been published! .In this study, we revealed the mechanism by which the efficient transcription by RNA polymerase II is accomplished on nucleosomes containing a histone variant H2A.B. #cryoEM.
embopress.org
imageimageHistone variants are essential regulators of gene expression. This study demonstrates that the histone variant H2A.B enhances transcription efficiency in the nucleosome, with the proximal...
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Check out our new preprint on H3-H4 octasome transcription by RNAPII!.We discovered that H3-H4 octasome is transcribed more efficiently than nucleosomes and visualized its transcription process by cryo-EM. #cryoEM.
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Check out our paper on the cryo-EM analysis of chromatin derived from human cells! .We have established a technically accessible method for analyzing the chromatin structure prepared from human cells.
onlinelibrary.wiley.com
We have established a method for the cryo-EM structural analysis of native mono- and poly-nucleosomes extracted from human cells. Single particle cryo-EM and cryo-electron tomography analyses have...
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Check out the cryo-EM structure of the CENP-A-H4 octasome. This nucleosome-like structure contains a histone octamer composed solely of centromere specific histone variant, CENP-A, and H4!. Amazing work by @NozawaL! Congratulations! š. #Subnucleosome.
onlinelibrary.wiley.com
Cryo-EM structure of the CENP-AāH4 octasome, which lacks H2A-H2B, was determined at 3.66 Ć
. The CENP-AāH4 octasome contains twice the amount of CENP-A compared to the canonical CENP-A nucleosome. It...
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Our paper, āThe cryo-EM structure of full-length RAD52 protein contains an undecameric ring,ā is among the top 10 most-cited papers in FEBS Open Bio (2023)!. Great collaboration with Kagawa-lab (Meisei Univ.)ācongrats, Kagawa-group!. š #CryoEM #RAD52.
febs.onlinelibrary.wiley.com
The cryo-EM structure of the human DNA repair protein RAD52 was determined at near-atomic resolution, which revealed that the full-length protein oligomerises into an undecameric ring. The N-termin...
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Excited to share our paper on the RNAPII-NELF-DSIF-TFIIS-nucleosome complex publishedĀ @ScienceAdvancesĀ ,Ā in collaboration with the Sekine labĀ @RIKEN_BDRĀ !Ā This study reveals how NELF and nucleosome function in promoter-proximal pausing ofĀ RNAPII!Ā
science.org
Structural and biochemical analyses elucidate how NELF and the +1 nucleosome are involved in promoter-proximal pausing of RNAPII.
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Check out our paper on the chromatin protein DEK published @NatureSMB! We found DEK as a nucleosome binding protein and its role in promoting H3K27me3 by PRC2! Great collaboration with Gotoh Lab, @YusukeKishi1 , MasumotoG, and @Cell_Tokyo_Tech ! Thank you!
nature.com
Nature Structural & Molecular Biology - Here the authors reveal that oncoprotein DEK binds the nucleosome, colocalizes with H3 K27 trimethylation and stimulates Polycomb repressive complex 2...
Super excited to share our work on the chromatin-associated oncoprotein DEK published in @NatureSMB!!š We found DEK as a nucleosome binding protein that facilitates H3K27me3 by PRC2 through chromatin reorganization!! Check out!
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With collaboration with Sugiyama lab(Kyoto Univ.), Our work regarding Cryo-EM and SAXS analysis of overlapping dinucleosome has been published!.
academic.oup.com
Abstract. Nucleosome remodelers modify the local structure of chromatin to release the region from nucleosome-mediated transcriptional suppression. Overlap
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A new paper has been published! Congratulations to the Uemura lab (Univ of Tokyo) and Takada lab (Kyoto Univ) for our collaborative work on observing nucleosome unwinding using solid-state nanopores!.
nature.com
Communications Biology - Research combining molecular dynamics simulations and solid-state nanopore measurements reveals distinct disassembly pathways that may explain the distinct properties and...
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RT @osakabe_a: Very excited to share that our new work is finally outš.We demonstrate that the chromatin remodeling factor DDM1 āopensā theā¦.
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Check out our latest research on chromatin remodeler DDM1 and the H2A.W nucleosome. We were able to visualize how DDM1 opens the the H2A.W nucleosome! This is a great collaboration with Drs Akihisa Osakabe and Tetsuji Kakutani. Congratulations!.
nature.com
Nature Communications - Osakabe and colleagues report the cryo-EM structures of Arabidopsis nucleosomes and how they complex with the chromatin remodeler DDM1, providing insights into how DDM1...
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Our new paper about nucleosome containing H3E97K mutation is published! This mutation is found in cancer cells.
onlinelibrary.wiley.com
Cryo-EM structure of the nucleosome containing the H3 E97K mutation was determined. The H3 E97K mutation enhances the flexibility of the nucleosomal DNA ends. The H3 E97K mutation affects the linker...
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