Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes

Wells, Jennifer N. and Buschauer, Robert and Mackens-Kiani, Timur and Best, Katharina and Kratzat, Hanna and Berninghausen, Otto and Becker, Thomas and Gilbert, Wendy and Cheng, Jingdong and Beckmann, Roland and Cate, Jamie H. D. (2020) Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes. PLOS Biology, 18 (7). e3000780. ISSN 1545-7885

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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.

Item Type: Article
Subjects: Eurolib Press > Biological Science
Depositing User: Managing Editor
Date Deposited: 21 Feb 2023 06:27
Last Modified: 16 Apr 2024 04:09
URI: http://info.submit4journal.com/id/eprint/1195

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