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.
- Mtinie
> There are people who will tell you that a cell is just the way that ribosomes make more ribosomes, and I’m not in a position to say that they’re wrong. It’s for sure that these protein-synthesizing factories are extremely ancient, extremely well-optimized, and they’re constantly at work in every living cell reading off sequences from messenger RNA molecules and extruding the corresponding protein sequences.
I recognize that our bodies are biomechanics in action. I’ve read this multiple times over the years. But there’s something fresh (to me) in the way Dr. Lowe describes them as (paraphrasing): “ancient technology, in use, today”.
It’s both a comfort and a curse as I think about it from this perspective.
- MarkusQ
Finding a cogent explanation for yet another category of "junk-DNA"/non-coding region is quite encouraging. Yes, things are turning out to be more complicated than we thought, but they are also more comprehensible than we feared, at least once we figure out the right way to look at things.
- kazinator
My joints may be inflexible, but at least I can't be misfolded!