EMD-11099

Single-particle
3.1 Å
EMD-11099 Deposition: 28/05/2020
Map released: 29/07/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-11099

Cryo-EM structure of human 80S ribosomes bound to EBP1, eEF2 and SERBP1

EMD-11099

Single-particle
3.1 Å
EMD-11099 Deposition: 28/05/2020
Map released: 29/07/2020
Last modified: 22/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: 80S ribosome bound to EBP1, eEF2 and SERBP1
Fitted models: 6z6m (Avg. Q-score: 0.474)

Deposition Authors: Wells JN , Buschauer R
Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.
Wells JN , Buschauer R, Mackens-Kiani T, Best K, Kratzat H, Berninghausen O , Becker T, Gilbert W , Cheng J, Beckmann R
(2020) PLoS Biol , 18 , e3000780 - e3000780
PUBMED: 32687489
DOI: doi:10.1371/journal.pbio.3000780
ISSN: 1545-7885
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.