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Visualizing TERRA RNA G-quadruplex Unfolding in FUS Biomolecular Condensates.

Tongyin Zheng1, Nicolas L Fawzi1

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RNA G-quadruplexes (rG4s) are stable structures. FUS protein condensates can unfold these RNA G-quadruplexes, explaining their variable stability within cells.

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FUSNMR spectroscopyRNA G-quadruplexbiomolecular condensatesphase separationtelomere RNA

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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.