Abstract
Adaptation to physiological stimuli is a critical area of research that allows us to understand how biological processes relate to development, neurodegenerative disorders and cancer. Cells can acclimatize and survive in stressful settings by various means, including the formation of biomolecular condensates. These membrane-less cellular bodies facilitate basic biochemical processes, including transcription and DNA replication. While liquid-like condensates have been attributed various functions, solid- like condensates are generally perceived as amorphous sites of protein storage. Here, we show that key ribosomal proteins and translation factors relocalize from the cytoplasm to nuclear solid-like Amyloid-bodies in cells responding to physiological stressors. These participants of the cytoplasmic protein synthesis machinery form translationally active ribosomes along fiber-like assemblies of Amyloid-bodies to sustain local nuclear protein synthesis (LNPS). Transcriptome analysis of Amyloid-bodies identified mature mRNA transcribed by the Heat Shock Factor 1. Depletion of stress-induced ribosomal intergenic spacer noncoding RNA that construct Amyloid-bodies prevents recruitment of the nuclear protein synthesis machinery, abolishes LNPS and impairs the nuclear stress response. We propose that Amyloid-bodies support local nuclear translation during stress and that solid-like condensates can facilitate complex biochemical reactions alike their liquid counterparts.