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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

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G-quadruplexes rescuing protein folding.

Ahyun Son1, Veronica Huizar Cabral1, Zijue Huang1

  • 1Department of Chemistry & Biochemistry, Knoebel Institute for Healthy Aging, University of Denver, Denver, CO 80208.

Proceedings of the National Academy of Sciences of the United States of America
|May 8, 2023
PubMed
Summary
This summary is machine-generated.

G-quadruplex (G4) nucleic acids accelerate protein folding by rescuing intermediates. In Escherichia coli, G4s improve protein folding quality rather than preventing aggregation.

Keywords:
G4protein foldingproteostasisquadruplex

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Cellular proteome health is vital.
  • G-quadruplex (G4) nucleic acids are known to prevent protein aggregation in vitro.
  • The role of G4s in protein folding remained unexplored.

Purpose of the Study:

  • To investigate the role of G-quadruplexes in protein folding.
  • To determine if G4s can influence protein folding kinetics and quality.

Main Methods:

  • In vitro protein folding experiments were conducted.
  • Time-course folding experiments were performed in Escherichia coli.

Main Results:

  • G-quadruplexes were found to accelerate protein folding by rescuing kinetically trapped intermediates.
  • G4s facilitate the transition to both native and near-native folded states.
  • Experiments in E. coli showed G4s primarily enhance protein folding quality, not aggregation prevention.

Conclusions:

  • G-quadruplex nucleic acids can actively promote protein folding.
  • This suggests a significant role for nucleic acids in cellular protein folding.
  • Nucleic acids and ATP-independent chaperones may dictate protein folding outcomes.