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-Structure paper
Title | A small ribosome-associated ncRNA globally inhibits translation by restricting ribosome dynamics. |
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Journal, issue, pages | RNA Biol, Vol. 18, Issue 12, Page 2617-2632, Year 2021 |
Publish date | Jun 13, 2021 |
Authors | Julia Reuther / Lukas Schneider / Ioan Iacovache / Andreas Pircher / Walid H Gharib / Benoît Zuber / Norbert Polacek / |
PubMed Abstract | Ribosome-associated non-coding RNAs (rancRNAs) have been recognized as an emerging class of regulatory molecules capable of fine-tuning translation in all domains of life. RancRNAs are ideally suited ...Ribosome-associated non-coding RNAs (rancRNAs) have been recognized as an emerging class of regulatory molecules capable of fine-tuning translation in all domains of life. RancRNAs are ideally suited for allowing a swift response to changing environments and are therefore considered pivotal during the first wave of stress adaptation. Previously, we identified an mRNA-derived 18 nucleotides long rancRNA (rancRNA_18) in that rapidly downregulates protein synthesis during hyperosmotic stress. However, the molecular mechanism of action remained enigmatic. Here, we combine biochemical, genetic, transcriptome-wide and structural evidence, thus revealing rancRNA_18 as global translation inhibitor by targeting the E-site region of the large ribosomal subunit. Ribosomes carrying rancRNA_18 possess decreased affinity for A-site tRNA and impaired structural dynamics. Cumulatively, these discoveries reveal the mode of action of a rancRNA involved in modulating protein biosynthesis at a thus far unequalled precision. |
External links | RNA Biol / PubMed:34121604 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.4 - 5.1 Å |
Structure data | EMDB-12986: EMDB-12988: |
Source |
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