Rapidly proliferating cells are at risk of compromised cell fitness due to proteostasis collapse from perturbations that interfere with ribosome biogenesis.

High-resolution maps and models of the bacterial ribosome provide new chemical insights into protein synthesis, and should enable the development of robust tools for cryo-EM structure modeling and refinement.

Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.

The anticonvulsant drug lamotrigine inhibits bacterial ribosome biogenesis and reveals an unexplored role for initiation factor 2 (IF2) in ribosome assembly.

BUD23 links ribosome function with mitochondrial protein expression and efficient oxidative phosphorylation by promoting selective mRNA translation and is therefore critical to mouse development and postnatal cardiac function.

The molecular mechanism behind how emetine inhibits the ribosome of the human malaria parasite, along with structural details of the complex formed, is revealed at high resolution using cryo-electron microscopy.

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.

Ribosomes translate through stop codons far more often than previously thought, yielding C-terminally extended proteins in a variety of eukaryotes.

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

Although puromycin staining is often used to examine subcellular translation, puromycin-labeled proteins are rapidly released from ribosomes even in the presence of elongation inhibitors, which may confound translation site localization.