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.

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.

Biochemical, biophysical, and structural approach to determine the molecular basis of the calcium-sensitive regulation of the Gα chaperone and guanine exchange factor Ric-8A by the neuronal calcium sensor NCS-1.

Multiple mechanisms, by which a highly conserved chromatin-remodeling factor RSC facilitates initiation and maintenance of large-scale, rapid gene expression upon exit from quiescent state, have been discovered.

Cryo-EM shows a 5’ DNA site on the RFC clamp loader, in addition to the 3’ site, and biochemical study shows the 5’ site facilitates PCNA loading onto gaps, consistent with genetics indicating the 5’ DNA site facilitates gap repair.

A combination of genetics, expression, genomic localization, and genomic nucleosome profiling demonstrates antagonism between two chromatin remodelers that reveal different mechanisms at different promoter architectures.

Structural, biochemical, and cellular data reveal the mechanism by which the clamp loader attaches sliding clamps at gapped and nicked DNA to support DNA damage repair.

Single-particle imaging of RSC and ISW2 chromatin remodelers on DNA stretched between dual optical tweezers reveals distinctive 1D diffusion and opposing push–pull nucleosome translocation on engagement with sparse nucleosome arrays.

The structure of the yeast RSC complex, a member of the SWI/SNF chromatin remodeling family, determined by cryo-electron microscopy, reveals a conserved structural core and the mode of nucleosome engagement.

Single molecule FRET reveals that the SWI/SNF-family remodeling enzyme RSC translocates nucleosomes along the DNA in steps of ~1-2 base pairs in size.