2. Academic Validation
  3. SNOR promotes translation restart after dormancy

SNOR promotes translation restart after dormancy

  • Nature. 2026 May 13. doi: 10.1038/s41586-026-10530-7.
Maciej Gluc # 1,  Higor Rosa # 2 3,  Maria Bozko 1,  Lesley A Turner 4,  Cassidy R Prince 5,  Yelena Peskova 1,  Heather A Feaga 5,  Kathleen L Gould 4,  Simone Mattei 6 7,  Ahmad Jomaa 8 9
Affiliations

Affiliations

  • 1 Department of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, University of Virginia, Charlottesville, VA, USA.
  • 2 Molecular Systems Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
  • 3 Collaboration for joint PhD degree, Faculty of Biosciences, EMBL and Heidelberg University, Heidelberg, Germany.
  • 4 Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN, USA.
  • 5 Department of Microbiology, Cornell University, Ithaca, NY, USA.
  • 6 Molecular Systems Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany. [email protected].
  • 7 EMBL Imaging Centre, European Molecular Biology Laboratory, Heidelberg, Germany. [email protected].
  • 8 Department of Molecular Physiology and Biological Physics and Center for Cell and Membrane Physiology, University of Virginia, Charlottesville, VA, USA. [email protected].
  • 9 Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA. [email protected].
  • # Contributed equally.
PMID: 42129552 DOI: 10.1038/s41586-026-10530-7
Abstract

Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis1-4. How inactive eukaryotic ribosomes are reactivated when nutrients return remains unclear. Here, using high-resolution in situ cryo-electron tomography in Schizosaccharomyces pombe, we identify SNOR, an SBDS domain-containing ribosome-associated factor that binds at the peptidyl transferase centre and contacts the hypusinated loop of eIF5A during glucose depletion-induced dormancy. Rather than acting as a canonical hibernation factor, SNOR licenses dormant ribosomes for rapid translational restart. Upon glucose repletion, SNOR and eIF5A act together to promote efficient recovery of polysomes and exit from dormancy. These findings define a stress-responsive ribosome restart module that couples carbon-source limitation to surveillance of the ribosomal active site and reactivation of protein synthesis.

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