Proteome-wide profiling reveals compartment-specific RNA buffering of protein aggregation during stress

Heat and salt stress in Saccharomyces cerevisiae causes a stress-specific RNA interactome reorganization, with many proteins shifting into high-molecular-weight, RNase-sensitive aggregation fractions.

• Why it matters: Stress adaptation depends on RNA remodeling and condensate assembly, but the global, RNA-dependent reorganization of macromolecular RNA–protein assemblies across compartments is not well mapped.
• What they did: Using R-DeeP, a density-gradient workflow with quantitative mass spectrometry, the study profiled RNA-dependent sedimentation of the yeast proteome during heat and salt stress, with and without RNase treatment.
• The result: Nuclear proteins are partially shielded from stress-induced aggregation, linked to stress-driven nuclear RNA retention from blocked RNA export and abolished by RNase, while cytoplasmic proteins show increased aggregation.

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