Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes

Poepsel, Simon; Kasinath, Vignesh; Nogales, Eva

doi:10.1038/s41594-018-0023-y

Title: Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes

Journal Article · Mon Jan 29 00:00:00 EST 2018 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/s41594-018-0023-y· OSTI ID:1490278

^[1]; Kasinath, Vignesh ^[1];

^[2]

Univ. of California, Berkeley, CA (United States). California Inst. for Quantitative Biology (QB3); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrative Bio-Imaging Div.
Univ. of California, Berkeley, CA (United States). California Inst. for Quantitative Biology (QB3), Howard Hughes Medical Inst., and Dept. of Molecular and Cell Biology; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Molecular Biophysics and Integrative Bio-Imaging Div.

Epigenetic regulation is mediated by protein complexes that couple recognition of chromatin marks to activity or recruitment of chromatin-modifying enzymes. Polycomb repressive complex 2 (PRC2), a gene silencer that methylates lysine 27 of histone H3, is stimulated upon recognition of its own catalytic product and has been shown to be more active on dinucleosomes than H3 tails or single nucleosomes. These properties probably facilitate local H3K27me2/3 spreading, causing heterochromatin formation and gene repression. Here, cryo-EM reconstructions of human PRC2 bound to bifunctional dinucleosomes show how a single PRC2, via interactions with nucleosomal DNA, positions the H3 tails of the activating and substrate nucleosome to interact with the EED subunit and the SET domain of EZH2, respectively. We show how the geometry of the PRC2–DNA interactions allows PRC2 to accommodate varying lengths of the linker DNA between nucleosomes. Furthermore, our structures illustrate how an epigenetic regulator engages with a complex chromatin substrate.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States). National Energy Research Scientific Computing Center (NERSC)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1490278

Journal Information:: Nature Structural & Molecular Biology, Vol. 25, Issue 2; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 117 works

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