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• W2887128430 endingPage "1121" @default.
• W2887128430 startingPage "1115" @default.
• W2887128430 abstract "To survive under conditions of stress, such as nutrient deprivation, bacterial 70S ribosomes dimerize to form hibernating 100S particles1. In γ-proteobacteria, such as Escherichia coli, 100S formation requires the ribosome modulation factor (RMF) and the hibernation promoting factor (HPF)2-4. Here we present single-particle cryo-electron microscopy structures of hibernating 70S and 100S particles isolated from stationary-phase E. coli cells at 3.0 Å and 7.9 Å resolution, respectively. The structures reveal the binding sites for HPF and RMF as well as the unexpected presence of deacylated E-site transfer RNA and ribosomal protein bS1. HPF interacts with the anticodon-stem-loop of the E-tRNA and occludes the binding site for the messenger RNA as well as A- and P-site tRNAs. RMF facilitates stabilization of a compact conformation of bS1, which together sequester the anti-Shine-Dalgarno sequence of the 16S ribosomal RNA (rRNA), thereby inhibiting translation initiation. At the dimerization interface, the C-terminus of uS2 probes the mRNA entrance channel of the symmetry-related particle, thus suggesting that dimerization inactivates ribosomes by blocking the binding of mRNA within the channel. The back-to-back E. coli 100S arrangement is distinct from 100S particles observed previously in Gram-positive bacteria5-8, and reveals a unique role for bS1 in translation regulation." @default.
• W2887128430 created "2018-08-22" @default.
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• W2887128430 date "2018-09-03" @default.
• W2887128430 modified "2023-10-13" @default.
• W2887128430 title "Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1" @default.
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• W2887128430 doi "https://doi.org/10.1038/s41564-018-0237-0" @default.
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• W2887128430 hasPublicationYear "2018" @default.
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