Reference - PMID:42129552 - SNOR promotes translation restart after dormancy.

Reference summary

PubMed ID

PMID:42129552

Title

SNOR promotes translation restart after dormancy.

Authors

Gluc M, Rosa H, Bozko M, Turner LA, Prince CR, Peskova Y, Feaga HA, Gould KL, Mattei S, Jomaa A

Citation

Nature 2026 May 13;

Publication year

2026

Abstract

Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis 1-4 . 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.

Annotation