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G-quadruplexes rescuing protein folding.

Ahyun SonVeronica Huizar CabralZijue HuangTheodore J LitbergScott Horowitz
Published in: Proceedings of the National Academy of Sciences of the United States of America (2023)
Maintaining the health of the proteome is a critical cellular task. Recently, we found G-quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in vitro and could at least indirectly improve the protein folding environment of Escherichia coli . However, the roles of G4s in protein folding were not yet explored. Here, through in vitro protein folding experiments, we discover that G4s can accelerate protein folding by rescuing kinetically trapped intermediates to both native and near-native folded states. Time-course folding experiments in E. coli further demonstrate that these G4s primarily improve protein folding quality in E. coli as opposed to preventing protein aggregation. The ability of a short nucleic acid to rescue protein folding opens up the possibility of nucleic acids and ATP-independent chaperones to play considerable roles in dictating the ultimate folding fate of proteins.
Keyphrases
  • single molecule
  • escherichia coli
  • protein protein
  • molecular dynamics simulations
  • amino acid
  • mental health
  • nucleic acid
  • risk assessment
  • pseudomonas aeruginosa
  • healthcare
  • biofilm formation