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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.
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.
Elango et al. identify a new class of substrates on which the Fanconi anemia SLX4–XPF nuclease operates to mediate homologous recombination at DNA–protein replication fork barriers and promote cellular tolerance of DNA–protein cross-links.
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.
Functional assays and cryo-EM structures show that ubiquitin binding and a cofactor drive protein quality-control client selection by the hybrid E2/E3 enzyme UBE2O.
Here, the authors find that histone demethylase Epe1-mediated stress resistance is regulated by proteasome-dependent truncation, allowing heterochromatin to reprogram gene expression that confers antifungal resistance to some fission yeast cells in the population.
Cryo-EM, X-ray crystallography and crosslinking mass spectrometry are harnessed to solve the structure of the full-length Rho-GEF P-Rex1, uncovering a two-layered mechanism of autoinhibition released upon Gβγ and PI(3,4,5)P3 binding.
This work reveals the structural and biochemical basis for phosphorylation-dependent day/night signaling by KaiC in the cyanobacterial circadian clock.
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.
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.
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.
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.
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.
Here authors visualize dynamics GAGA pioneer factor (GAF) association with chromatin in vivo in Drosophila hemocytes. The characterization of GAF kinetics provides a temporal mechanism for maintenance of open chromatin for transcriptional responses to homeostatic, environmental and developmental signals.
This comprehensive study of the most enigmatic serotonin receptor 5-HT5AR includes lots of pharmacological investigations, inactive and active state structures with antagonist, partial agonist and full agonists. Also, a highly potent and selective antagonist was developed.
Multiple cryo-EM structures of human glycogen synthase reveal the basis of inhibition by phosphorylation and allosteric activation by glucose-6-phosphate.
Cryo-EM analysis of the human apelin receptor activated by either the endogenous peptide ligand or a potent synthetic small-molecule agonist reveals a mixture of homodimer and monomer organizations shedding light on a versatile regulation mechanism.