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

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

Inhibition of bacterial protein synthesis by an antimicrobial peptide apidaecin triggers translation arrest at the stop codons, ribosome queuing and pervasive stop codon readthrough.

A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.

Cells resolve unassigned codons with near-cognate suppression, frameshifting, and ribosomal rescue mechanisms, demonstrating that unassigned codons are permissible in both natural and engineered genetic codes as barriers to horizontal gene transfer.

Cue2 is an endonuclease that cleaves mRNA in the A site of the lagging ribosome upon ribosome collision events.

The cotranslational membrane integration of three multispanning Escherichia coli inner membrane proteins is followed using force profile analysis, uncovering unexpected complexities in the membrane integration process.

Endothelial Differentiation Factor 1 (EDF1) plays a critical role in driving mRNA-specific quality control and global transcriptional responses in response to ribosome collisions.

Proteins can fold deeper inside ribosomes with an enlarged exit tunnel.

Without ribosome recycling factor, ribosomes in Escherichia coli accumulate in 3'-UTRs and queue upstream of stop codons, but no effects were observed on the translational coupling of neighboring genes.