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TitleH2A Ubiquitination Alters H3-tail Dynamics on Linker-DNA to Enhance H3K27 Methylation.
Journal, issue, pagesJ Mol Biol, Vol. 435, Issue 4, Page 167936, Year 2023
Publish dateFeb 28, 2023
AuthorsHideaki Ohtomo / Shinsuke Ito / Nicholas J McKenzie / Michael Uckelmann / Masatoshi Wakamori / Haruhiko Ehara / Ayako Furukawa / Yasuo Tsunaka / Marika Shibata / Shun-Ichi Sekine / Takashi Umehara / Chen Davidovich / Haruhiko Koseki / Yoshifumi Nishimura /
PubMed AbstractPolycomb repressive complex 1 (PRC1) and PRC2 are responsible for epigenetic gene regulation. PRC1 ubiquitinates histone H2A (H2Aub), which subsequently promotes PRC2 to introduce the H3 lysine 27 ...Polycomb repressive complex 1 (PRC1) and PRC2 are responsible for epigenetic gene regulation. PRC1 ubiquitinates histone H2A (H2Aub), which subsequently promotes PRC2 to introduce the H3 lysine 27 tri-methyl (H3K27me3) repressive chromatin mark. Although this mechanism provides a link between the two key transcriptional repressors, PRC1 and PRC2, it is unknown how histone-tail dynamics contribute to this process. Here, we have examined the effect of H2A ubiquitination and linker-DNA on H3-tail dynamics and H3K27 methylation by PRC2. In naïve nucleosomes, the H3-tail dynamically contacts linker DNA in addition to core DNA, and the linker-DNA is as important for H3K27 methylation as H2A ubiquitination. H2A ubiquitination alters contacts between the H3-tail and DNA to improve the methyltransferase activity of the PRC2-AEBP2-JARID2 complex. Collectively, our data support a model in which H2A ubiquitination by PRC1 synergizes with linker-DNA to hold H3 histone tails poised for their methylation by PRC2-AEBP2-JARID2.
External linksJ Mol Biol / PubMed:36610636
MethodsEM (single particle)
Resolution3.87 Å
Structure data

EMDB-32094: Cryo-EM structure of H2A-ubiquitinated nucleosome
Method: EM (single particle) / Resolution: 3.87 Å

Source
  • Homo sapiens (human)

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