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Updated: Jan 13, 2026
05:37
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
Published on: April 4, 2025
1.2K
Specificity of the stabilizing interaction between intrinsically disordered protein sequences and G-quadruplexes in
Lachlan B Cox1,2, John S Mattick2,3, Isis A Middleton1,2
1School of Chemistry, University of New South Wales, Sydney, NSW 2052, Australia.
Nucleic Acids Research
|January 7, 2026
Summary
Intrinsically disordered regions (IDRs) selectively stabilize RNA G-quadruplexes (rG4s) through weak interactions. This RNA folding mechanism explains specific interactions and mutations in IDRs.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Intrinsically disordered regions (IDRs) are crucial for protein regulation and cellular processes.
- The RGG domain within IDRs interacts with RNA G-quadruplexes (rG4s), key regulatory RNA structures.
Purpose of the Study:
- To investigate the mechanism by which IDRs selectively bind and stabilize rG4 structures.
- To elucidate how IDRs achieve specificity in RNA G4 interactions.
Main Methods:
- Utilized weak binding interactions between RGG-rich peptides and rG4s.
- Employed multidimensional NMR and circular dichroism (CD) spectroscopy.
Main Results:
- Demonstrated that IDRs selectively template and stabilize the human telomeric TERRA rG4.
- Showed that specific nucleotide and amino acid identities dictate RGG peptide-rG4 interaction specificity.
- Identified a novel RNA folding pathway independent of high-affinity binding or monovalent cations.
Conclusions:
- IDRs can selectively recognize RNA G4s over DNA G4s due to specific sequence determinants.
- The findings explain the high specificity of IDR-rG4 interactions in vivo and the prevalence of monogenic mutations in IDRs.
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