Heat shock induces silent ribosomes and reorganizes mRNA turnover
mRNAs associate with single or multiple ribosomes; these ribosomal assemblies —monosomes and polysomes — translate the mRNAs before degradation. The impact of heat stress on this mRNA turnover remains unclear. In heat-shocked yeast cells, the proportion of monosomes within the ribosomal assemblies rises without a corresponding increase in the number of mRNAs associated with them. As a result, most monosomes are devoid of mRNAs and silent, lacking translational initiation factors and proteins facilitating posttranslational folding. The accumulation of silent ribosomes generally reduces the rate of association of transcripts with the ribosomes. However, elevated temperatures enhance the ribosomal association of specific mRNAs, primarily those encoding heat-shock proteins, allowing them to balance their increased degradation rates. Additionally, reduced binding of the Xrn1 exonuclease to mRNAs diminishes the influence of codon optimality on mRNA stability. These mechanisms reconfigure the translation machinery to prioritize heat-shock protein synthesis over ribosome biogenesis. Overall design: We carried out polysome profiling of yeast BY4743 strains, at standard conditions and heat shock (30°C and 42°C), and carried out RNASeq without rRNA depletion of each of the pools with them corresponding to specific ribosomal complexations of mRNA.