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During eukaryotic ribosome biogenesis, the nascent 60S subunit is activated by SBDS and GTPase EFL1. Cryo-EM and mutational analyses reveal how SBDS–EFL1 evicts antiassociation factor eIF6 from 60S and explain the effects of disease-related SBDS mutations.
Solid-state and solution NMR spectroscopy provide insights into the chaperone αB-crystallin's highly dynamic assembly, which is instrumental in its distinct interactions with a wide range of structurally variable clients.
The E. coli GTPase HflX promotes ribosomal-subunit dissociation by inducing conformational changes in central intersubunit bridges and thereby rescues stalled ribosomes under heat-shock conditions.
New crystal structures of the human endonuclease APE1 bound to substrate and product DNAs reveal the mechanism of recognition and processing of apurinic-apyrimidinic (AP) sites during base excision repair.
The crystal structure of a prokaryotic proton-driven fumarate transporter, the first for the diverse SLC26 transporter family, reveals a rare transmembrane-segment topology. The opposite orientation of two short central helices leads to the formation of a dipole-mediated anion-binding site, which is made alternately accessible to either side of the membrane through the rocking movement of the core and gate domains of the transporter.
Sharing source data—the actual measurements and unprocessed images behind the graphical representations used in figures—helps to ensure transparency and reproducibility of research results. We urge our authors to submit and share the source data with their published papers.
How is cellular cargo delivered at the right time and the right place, in response to the right signal? A key new piece in this fascinating biological puzzle has just been revealed.
The cellular 'alarmone' molecule ZTP accumulates when a critical cellular metabolic pathway is starved for substrate. The high-resolution structure of ZTP bound to its RNA-based sensor reveals unexpected strategies used by RNA to specifically recognize small-molecule ligands within the complex cellular mixture.
New analyses in S. pombe show that both the leading and lagging strands are replicated by DNA polymerase δ when stalled replication forks use homologous recombination to restart semiconservative DNA synthesis.
ChIP-seq, biochemical and in vivo assays show that Rif1 binds G-rich motifs that can form G-quadruplex structures, thus regulating firing of proximal and distal DNA replication origins in fission yeast.
A crystal structure of the RNA-binding domain of Tetrahymena telomerase reverse transcriptase (TERT) with its template RNA (TER) reveals interactions that establish the template boundary element and direct the addition of telomeric DNA repeats.
Concentrations of cations and ATP affect the binding activities of synaptotagmin-1, to trigger synaptic vesicle exocytosis. In physiological ionic conditions, synaptotagmin-1's interaction with SNARE proteins is prevented, and its binding is confined to PIP2-containing membrane.
Solution NMR and functional analyses reveal the 3D structure of a transmembrane reductase, the archeal CcdA, and suggest a mechanism for how these enzymes relay electrons across cell membranes.
Foot-and-mouth disease virus (FMDV) capsids are often unstable, thus limiting their use as vaccines. A computational method was used to strengthen protein-protein interfaces and engineer stabilized FMDV capsids, which generated improved antibody responses in vaccinated calves and guinea pigs.
In somatic cells, L1 retrotransposition is kept in check by DNA methylation. However, in hypomethylated cells, such as cancer cells or iPSCs, miR-128 represses new retrotransposition events and thus might aid in maintaining genome stability.
SLC26 membrane proteins constitute a large family of anion transporters with diverse functions. The first structure of a full-length SLC26 transporter now provides a common framework for the architecture of this protein family.
An in vitro–reconstitution approach reveals the interactions between nuclear pore complex modules. Short motifs within linker nucleoporins connect the inner-pore-ring complex with subcomplexes of the outer ring and the transport channel.
Cryo-EM analysis of a bacterial SRP reveals that, differently from eukaryotic SRP, it interacts with the ribosome via contacts between the 6S RNA and the 23S rRNA to mediate translational slowdown.
AFM and NMR are used to observe how the chaperones Skp and SurA work to fold a β-barrel outer-membrane protein, FhuA. Skp maintains FhuA in an unfolded state, and Sur A facilitates its folding.