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.

Rqc2-mediated modification of ribosome-stalled nascent chains with "CAT tails" promotes formation of insoluble aggregates suggesting that proteins can become specifically marked for aggregation.

A genome-wide screen in yeast reveals that key proteins in ribosome quality control also regulate mutant Huntingtin aggregation and toxicity.

Analysis of neo-splicetope-specific T cell responses strongly questions the idea that in vitro proteasome-catalyzed peptide splicing reaction simulates the in vivo situation with the same high fidelity as the in vitro generation of non-spliced epitopes.

A SWI/SNF-family chromatin remodeling subcomplex from yeast is identified (RSC1) that is specialized to slide nucleosomes residing on DNA sequences that confer partial nucleosome unwrapping, with assistance from accessory factors.

The enzyme that collaborates with ubiquitin ligases to promote the release of defective polypeptides from stalled ribosomes in a process named ribosome-associated degradations has been identified as the ATPase Cdc48.

Rather than acting as passive and neutral co-factors for proneural proteins, E proteins play an active role in modulating the way the distinct proneural proteins instruct neurogenesis.

A hierarchical relationship among highly conserved regulatory ribosomal ubiquitylation events and the presence of antagonistic deubiquitylating enzymes suggests a dynamic ubiquitin code impacts ribosome-associated activities.

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

Ribosome collisions along an mRNA are shown to recruit factors that prevent additional ribosomes from initiating translation on that mRNA, thereby providing time to resolve the collision.