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- Title
Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.
- Authors
Wells, Jennifer N.; Buschauer, Robert; Mackens-Kiani, Timur; Best, Katharina; Kratzat, Hanna; Berninghausen, Otto; Becker, Thomas; Gilbert, Wendy; Cheng, Jingdong; Beckmann, Roland
- Abstract
Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes. Single-particle cryo-EM structures of recently identified factors for eukaryotic ribosome hibernation, yeast Lso2 and its human counterpart bound to ribosomes, reveals that the factors bind in the intersubunit space. The study also explores how the structure of these complexes relates to the functional reactivation of translation by ribosome recycling.
- Subjects
RIBOSOMES; CARRIER proteins; GUANOSINE triphosphatase; HIBERNATION; YEAST
- Publication
PLoS Biology, 2020, Vol 18, Issue 7, p1
- ISSN
1544-9173
- Publication type
Article
- DOI
10.1371/journal.pbio.3000780