UTR-ly unexpected: RNA chaperones tame intrinsically disordered proteins.

How do cells ensure that complex, multidomain proteins fold correctly? Luo et al. reveal a self-contained solution. The 3' UTR of an mRNA co-translationally chaperones the protein it encodes, preventing intrinsically disordered regions from making inappropriate contacts. This functionality, localized to mesh-like condensates, challenges Anfinsen's dogma and opens therapeutic possibilities.
How do cells ensure that complex, multidomain proteins fold correctly? Luo et al. reveal a self-contained solution. The 3' UTR of an mRNA co-translationally chaperones the protein it encodes, preventing intrinsically disordered regions from making inappropriate contacts. This functionality, localized to mesh-like condensates, challenges Anfinsen's dogma and opens therapeutic possibilities.




