Ribosomes' Untranslated Regions Act as Chaperones to Keep Disordered Proteins from Folding
Preventing Misfolding by Preventing Folding
New research reveals that the 3' untranslated regions (UTRs) of mRNAs encoding intrinsically disordered proteins act as chaperones, preventing misfolding and aggregation during translation. These conserved sequences form mesh-like condensates that sequester the nascent protein, particularly for RNA-binding disordered proteins like Myc, Utx, and Jmjd3. The findings suggest Anfinsen's dogma may only apply to simpler proteins, as these UTRs represent a parallel system to traditional chaperones.
These unusual 3'UTRs are sort of a parallel universe to the well-known chaperones that assist with the folding of structured proteins.