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  • A study published in Nature Structural & Molecular Biology now unveils, at the atomic level, the initial mechanisms of prion toxicity, providing insights into the pathogenic mechanisms of a protein neurodegenerative disease caused by protein misfolding.

    • Jesús R. Requena
    News & Views
  • CST is both an ssDNA-binding complex and a DNA Pol-α/primase cofactor that coordinates the switch from G-strand elongation to C-strand fill-in during telomere maintenance. Four papers in Nature Structural & Molecular Biology and Nature provide transformative insights into CST activity, providing a platform to understand lagging-strand synthesis genome wide.

    • Conner L. Olson
    • Alexandra T. Barbour
    • Deborah S. Wuttke
    News & Views
  • The H-latch is a well-defined structural change occurring in PrPC bound to the neurotoxic antibody POM1, and its presence shows a positive correlation with neurotoxicity. Inhibition of the H-latch prolongs the lifespan of prion-diseased mice.

    • Karl Frontzek
    • Marco Bardelli
    • Adriano Aguzzi
    Article Open Access
  • Amplification of oncogene expression through extrachromosomal DNA is a common feature of many cancers and is associated with poor outcomes. Hung et al. review how regulation of extrachromosomal DNA gene expression is linked to alterations in chromatin structure and changes in contacts with DNA regulatory elements.

    • King L. Hung
    • Paul S. Mischel
    • Howard Y. Chang
    Review Article
  • An endogenous proteasome inhibitor was identified 30 years ago, but its mechanism remained unclear. Rawson et al. show that this inhibitor is present within the interior of the proteasome, where it simultaneously inhibits all six active sites.

    • Shaun Rawson
    • Richard M. Walsh Jr.
    • John Hanna
    Article
  • Clemons and colleagues identify a guided entry of tail-anchored proteins (GET) pathway in the pathogen Giardia intestinalis and characterize it structurally, revealing several previously unknown structures of the central protein Get3. The work resolves some important open questions and results in a comprehensive model for the insertion of tail-anchored membrane proteins.

    • Michelle Y. Fry
    • Vladimíra Najdrová
    • William M. Clemons Jr
    Article
  • Structural maintenance of chromosomes (SMC) complexes such as condensin regulate chromosome organization by extruding loops. A new study uses single-molecule imaging of condensin on supercoiled DNA to understand how condensins navigate the under- and overwound DNA states common throughout the genome.

    • Domenic N. Narducci
    • Anders S. Hansen
    News & Views
  • Two new papers describe the successful purification of the partially intact human native red blood cell band 3 multiprotein membrane complexes, providing information that the authors then use to capture the structures and interactions of multiple erythrocyte proteins using high-resolution cryo-EM.

    • Ashley M. Toye
    News & Views
  • Cryo-EM structures of human erythrocyte ankyrin-1 complex offer insights into the architecture of the RBC membrane and show how ankyrins can simultaneously recruit different membrane proteins to enable functional organization of membrane transport processes.

    • Francesca Vallese
    • Kookjoo Kim
    • Oliver Biggs Clarke
    Article
  • Single-molecule experiments reveal that condensin-induced DNA looping is stimulated by positive supercoils, and condensin preferentially binds near the tips of supercoiled plectonemes; upon loop extrusion, condensin collects nearby DNA plectonemes into a supercoiled loop.

    • Eugene Kim
    • Alejandro Martin Gonzalez
    • Cees Dekker
    Article