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Showing 1–4 of 4 results
Advanced filters: Author: Evan J. Worden Clear advanced filters

  • Yan et al. use cryo-EM to obtain structures that reveal how DNMT3A2 and DNMT3L cooperate to read histone signals and bind chromatin, illustrating a mechanism that controls DNA methylation and shapes epigenetic regulation.

    • Yan Yan
    • X. Edward Zhou
    • Ting-Hai Xu
    Research
    Nature Structural & Molecular Biology
    Volume: 33, P: 171-183

  • PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.

    • Evan J. Worden
    News & Views
    Nature Structural & Molecular Biology
    Volume: 32, P: 215-216

  • In the eukaryotic 26S proteasome, a heterohexameric AAA+ complex unfolds substrates prior to degradation. The yeast unfoldase subunits have now been expressed in bacteria and reconstituted into active proteasomes in vitro. Mutations of catalytic and structural motifs in each individual subunits reveal that they play distinct roles in substrate processing, peptidase binding and gate opening.

    • Robyn Beckwith
    • Eric Estrin
    • Andreas Martin
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1164-1172

  • Rpn11, the only essential deubiquitinase (DUB) of the 26S proteasome, sits at the top of the substrate entry pathway and facilitates substrate degradation through cotranslocational deubiquitination. The structure of the Rpn11–Rpn8 complex, together with functional assays, offers insight into Rpn11's promiscuous DUB activity during proteasomal degradation.

    • Evan J Worden
    • Chris Padovani
    • Andreas Martin
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 220-227