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Visualizing TERRA RNA G-quadruplex Unfolding in FUS Biomolecular Condensates
Tongyin Zheng1, Nicolas L Fawzi1
1Department of Molecular Biology, Cell Biology & Biochemistry and Robert J. and Nancy D. Carney Institute for Brain Science, Brown University, Providence, RI, USA.
Journal of Molecular Biology
|March 7, 2026
Summary
RNA G-quadruplexes (rG4s) are stable structures. FUS protein condensates can unfold these RNA G-quadruplexes, explaining their variable stability within cells.
Area of Science:
- Molecular Biology
- Biochemistry
- Structural Biology
Background:
- RNA G-quadruplexes (rG4s) are crucial regulatory structures in cells.
- Their in vivo behavior is debated due to detection challenges.
- TERRA is a model rG4 RNA known for its stability.
Purpose of the Study:
- To investigate the impact of FUS protein condensates on TERRA rG4 structure.
- To understand how phase separation affects RNA G-quadruplex stability in cellular environments.
Main Methods:
- Solution Nuclear Magnetic Resonance (NMR) spectroscopy.
- Studied interactions between FUS low-complexity/RGG domains (FUS LC-RGG1) and TERRA RNA.
- Utilized a mutant TERRA RNA as a control for unfolded RNA.
Main Results:
- FUS LC-RGG1 binds TERRA in dilute solution, perturbing but not disrupting the rG4 structure.
- Within FUS condensates, TERRA rG4 signatures disappear, indicating an unfolded conformation.
- At least one-third of TERRA RNA unfolds within FUS condensates, even in stabilizing buffer conditions.
Conclusions:
- Cellular condensates can destabilize RNA G-quadruplex structures.
- Phase separation by proteins like FUS can shift RNA structural ensembles towards unfolded states.
- This provides a mechanism for the observed variability in rG4 stability in vivo.
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