GTPBP7, NSUN4, and MTERF4 facilitate maturation of the peptidyl transferase center of the mitochondrial ribosome.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

The GTPase Nog1 orchestrates stalk assembly, peptidyl transferase centre maturation and polypeptide exit tunnel quality control.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

Directed evolution of the resistance enzyme Cfr under antibiotic selection identifies increased Cfr expression and stability as strategies to boost resistance and reveals that Cfr modification of the ribosome confers resistance by sterically occluding binding of antibiotics.

Yeast extracts recapitulate a quality-control pathway dedicated to rescuing stalled ribosomes, providing unexpected insights into a noncanonical elongation reaction and the fate of incompletely synthesized proteins.

Cryo-EM structures reveal the structural dynamics of ArfA*RF2-mediated rescue of stalled ribosomes.

With the removal of confounding artifacts, ribosome profiling can yield insight into the mechanism of protein synthesis in bacteria at high resolution.

Two integrated approaches shed light on how XBP1 arrest peptide induces intermediate level of translational pausing and identify hotspot positions to make it stronger.

The size of the mRNA fragment protected by a ribosome depends on the ribosome's conformation, which enables studies of the distinct steps of decoding and translocation at single-codon resolution.