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Identification of SFiNX, a complex of Nxf2–Nxt1, a variant of the mRNA export receptor Nxf1–Nxt1 and the Piwi-associated protein Panoramix, demonstrates an RNA export independent role for Nxf2 in piRNA-guided cotranscriptional transposon silencing.
The fly male germline stem cells undergo asymmetric division, with old histones H3 and H4 preferentially retained in the daughter stem cell. The mechanisms that contribute to this outcome are revealed using super-resolution microscopy and DNA fiber analyses.
A combination of biochemical, single-molecule, and in vivo assays reveals that the UV-DDB complex that removes UV-induced DNA lesions via the nucleotide excision repair pathway also promotes removal of oxidative lesions via base excision repair.
X-ray crystal structures of the full-length TcdB exotoxin of bacterial pathogen Clostridium difficile reveal pH-dependent conformational changes that allow translocation of the toxin from endosomes into the cytosol.
AAA+ ATPase spastin recognizes tubulin polyglutamylated C-terminal tails and severs microtubules. A cryo-EM structure of fly spastin with polyGlu reveals how spastin engages with the substrate, an activity allosterically coupled to nucleotide binding and oligomerization.
O-Mannosylation is an essential protein modification implicated in several diseases. Cryo-EM structures of the yeast mannosyltransferase complex Pmt1–Pmt2 bound to substrates reveal the substrate recognition model and confirm the reaction mechanism.
Cryo-EM structures of the active Cas9–sgRNA–DNA complex in the presence of Mg2+ capture Cas9 in the pre- and postcatalytic states as well as in the product-bound state, and reveal coupled domain motions and interactions between the enzyme and nucleic acids.
Transition metal FRET and Rosetta modeling reveal that the S4 helix in the voltage-sensing domain of the HCN channel moves downward and its carboxy-terminal portion tilts during hyperpolarization activation.
A CDK multisite phosphorylation code ensures that CDK can signal via hundreds of distinct targets to provide a temporally ordered phosphorylation pattern required for proper execution of the cell cycle.
The low-complexity domain of the RNA-binding protein FUS forms dynamic, multivalent interactions via multiple residue types and remains disordered in the densely packed liquid phase.
Crystal structures of the human HMCES SRAP domain in complex with DNA substrates demonstrate how the SRAP domain interacts with a variety of single-strand- and double-strand-containing DNA structures found at DNA-damage sites.
Crystal structures of human vasohibin 1 and 2 in complex with small vasohibin-binding protein (SVBP) in the absence and presence of different inhibitors and a C-terminal α-tubulin peptide define the structural basis of tubulin detyrosination.
A solid-state NMR structure of an amyloid fibril formed by synthetic human glucagon reveals two distinct β-strand conformations that alternate in an antiparallel fashion along the fibril axis.
Structures of human equilibrative nucleoside transporter 1 in complex with either dilazep or NBMPR reveal distinct inhibitory mechanisms of these drugs, providing insight for rational design of improved therapeutics modulating nucleoside transport.
Cryo-EM structures of fibrils formed by two segments from TDP-43 that are essential for aggregation of the full-length protein reveal fibril polymorphism and suggest mechanisms for pathogenesis.
HMCES protects abasic sites that block DNA replication via covalent protein attachment. Crystal structures of the Escherichia coli HMCES homolog YedK reveal that the conserved SRAP domain forms a thiazolidine linkage with the abasic site, explaining the stability of the DNA-protein cross-link and its specificity for DNA lesions at stalled replication forks.
Crystal structures of human VASH1–SVBP alone, in complex with a tyrosine-derived covalent inhibitor and bound to parthenolide, explain the requirement for SVBP during tubulin detyrosination and reveal the basis for substrate recognition.
The previously unknown human prenyltransferase, GGTase3, geranylgeranylates the ubiquitin ligase FBXL2, which bears a motif predicted to be recognized by GGTase1. The structure of the GGTase3–FBXL2–SKP1 complex reveals the basis of GGTase3 substrate specificity.
X-ray crystallography and cryo-EM analyses capture the influenza RNA polymerase with RNA primer-template at distinct steps of initiation and elongation, revealing changes in its active site that promote viral RNA synthesis.
Structures of PF846-stalled human ribosome nascent chain complexes show that this drug-like molecule binds in the ribosome exit tunnel in a eukaryotic-specific pocket formed by 28S rRNA and alters the path of the nascent polypeptide chain.