Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The ribosome-assembly factor Mrt4 prevents untimely recruitment of the RNA-export receptor Mex67–Mtr2 to the nascent 60S ribosomal subunit, thereby ensuring appropriately timed nuclear export.
Cryo-EM analyses of yeast TRiC (CCT) reveal conformational changes induced by ATP binding and a staggered mode of nucleotide binding to the different subunits.
The RNA-binding protein CPEB1 drives post-transcriptional changes in the host transcriptome and poly(A)-tail lengthening of viral RNAs, processes essential for productive HCMV infection.
Perinuclear localization of CED-3 zymogen in C. elegans germ cells and interaction with nuclear-pore protein NPP-14 inhibit autocatalytic activation of CED-3, a central event in apoptosis.
Analyses of Hsp90 mutants show no correlation between the speed of ATP turnover and chaperone activity in vivo, indicating that timing of conformational transitions, rather than cycle speed, is essential for Hsp90 function.
The structure of the S. pombe Dcp2–Dcp1 decapping enzyme complex with human activator PNRC2 and tight-binding cap analog reveals a new conformation and, along with kinetics analyses, provides insight into substrate recognition and mechanisms of activators.
The crystal structure of the Kluyveromyces lactis decapping enzyme complex Dcp1–Dcp2 is solved in the presence of activator Edc3 and reaction product m7GDP, revealing an active conformation of the enzyme.
A primate-specific insertion of an Alu element in 5S-OT, a lncRNA transcribed from 5S rRNA loci, allows 5S-OT to regulate alternative splicing via RNA-RNA pairing and recruitment of the splicing factor U2AF65.
The E4 ligase UFD-2 is required for apoptosis induced by DNA damage in C. elegans, and for the resolution of RAD-51 foci during homologous recombination-dependent repair, thus coordinating these two cellular processes.
Single-molecule spectroscopy reveals the complete mechanochemical cycle of the AAA+ protease ClpXP: ADP release and ATP binding occur during the dwell phase, whereas ATP hydrolysis and Pi release occur during the burst phase.
Structural, biochemical and functional analyses elucidate the mechanisms by which mutations in the TBC1D24 gene interfere with protein function, thus causing early-onset epilepsy and DOORS syndrome.
Structural and cross-linking analyses provide deeper insight into Zuo1's dual interactions with the ribosomal 60S and 40S subunits and indicate how Zuo1 may coordinate cotranslational protein folding and translation.
Structural elucidation and biochemical analysis of a cone snail insulin venom that binds and activates the human insulin receptor may permit design of ultrafast-acting insulin analogs for diabetes therapy.
Crystal structures of HIV Env trimer with native glycosylation in complex with neutralizing antibodies reveal a glycan shield of high-mannose and complex-type N-glycan and indicate a path for germline-targeting vaccine design.
Cryo-EM and mass spectrometry analyses of the spike glycoprotein trimer from coronavirus HcoV-NL63 reveal an extensive glycan shield that covers the protein surface, including an epitope targeted by neutralizing antibodies against several coronaviruses.
A systematic analysis reveals that acidic or phosphorylated residues upstream of the PDZ-binding motif contribute to efficient recognition of cargos by the SNX27 PDZ domain, thus leading to the identification of hundreds of potential new SNX27 ligands.
Cas1–Cas2 integrase achieves full-site integration only for proper targets and protospacers, whereas at non-CRISPR sites, integration stalls at the half-site intermediate, thereby protecting host genome integrity during CRISPR immune adaptation.
The structurally constrained knotted configuration of the RNA methyltransferase TrmD captures the free energy of substrate binding to facilitate catalysis.
The crystal structure of HIV-1 accessory protein Vpr in complex with human UNG2 and DDB1–DCAF1 provides insight into how the viral protein directs UNG2 for degradation.
One of the conserved proteins of the Staphylococcus aureus mobile genomic island responsible for methicillin resistance is an active MCM-like helicase, thus suggesting replication that would enhance the efficiency of horizontal gene transfer.