a b s t r a c tClusters of codons pairing to low-abundance tRNAs synchronize the translation with co-translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell-wide level remains elusive. Here we show that upregulation of three low-abundance tRNAs in Escherichia coli increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone-dependent proteins.

Background: Expansion of a polyglutamine repeat in atrophin-1 causes progressive neuronal dysfunction in neurodegenerative dentatorubropallidoluysian atrophy. Results: Nuclear inclusions of expanded atrophin-1 are more dynamic compared with the cytoplasmic aggregates. Conclusion: Structural variations of the aggregate core determine these dynamics. Significance: Probing the molecular properties of the inclusions is crucial for understanding the enhanced cellular toxicity of nuclear aggregates in polyglutamine pathologies.

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