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Updated: Apr 19, 2026
05:37
Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
Published on: April 4, 2025
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Characterizations of G-Quadruplex RNA-Protein Interactions in Living Cells.
Feng Tang1,2, Xiaochen Liang1, Douglas F Porter3
1Department of Chemistry, University of California, Riverside, California 92521, United States.
Analytical Chemistry
|April 17, 2026
Summary
Researchers developed G4-RaPID to identify RNA guanine quadruplex-interacting proteins (rG4IPs) in cells. This method revealed hnRNPA0 regulates NRAS mRNA translation by binding to rG4 structures.
Area of Science:
- Molecular Biology
- Genomics
- Biochemistry
Background:
- RNA guanine quadruplexes (rG4s) are crucial noncanonical structures involved in cellular functions and diseases.
- Identifying proteins interacting with rG4s (rG4IPs) is key to understanding their biological significance.
Purpose of the Study:
- To develop and validate G4-RaPID, a chemoproteomic strategy for unbiased profiling of rG4IPs in living cells.
- To identify novel rG4IPs and elucidate their roles in RNA regulation.
Main Methods:
- Development of G4-RaPID, a chemoproteomic platform based on RNA-protein interaction detection (RaPID).
- Application of G4-RaPID to profile rG4IPs across distinct rG4 sequences.
- Biochemical assays, CLIP-seq, and luciferase reporter assays to validate protein-rG4 interactions and functional consequences.
Main Results:
- G4-RaPID identified 105 candidate rG4IPs enriched across three rG4 sequences.
- hnRNPA0, CHD4, and IGF2BP1 were confirmed as direct rG4 binders.
- hnRNPA0 was shown to bind endogenous rG4s and negatively regulate NRAS mRNA translation via rG4 interaction.
Conclusions:
- G4-RaPID is a robust method for mapping rG4-protein interactions in living cells.
- hnRNPA0-rG4 recognition is a regulatory mechanism controlling NRAS mRNA translation.
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