ArticleNature microbiology2025
Structure of an archaeal ribosome reveals a divergent active site and hibernation factor.
Article in Nature microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A conserved archaeal protein with evolutionary links to bacterial ribosome hibernation and eukaryotic energy sensing.The EMBO journal · 2026Article
- SNOR promotes translation restart after dormancy.Nature · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.Nature communications · 2026Article
- RiboScreenBiomedicines · 2026Review
- A family of ribosome hibernation factors widespread in Archaea.Nature communications · 2026Article
- A Novel Eukaryotic Ribosome Factor Enables Translation Restart Following Cellular Dormancy.bioRxiv : the preprint server for biology · 2026Article
- Circularization of 23S rRNA but not 16S rRNA within archaeal ribosomes.Genome biology · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.bioRxiv : the preprint server for biology · 2026Article
- Article
- Cryo-EM study and in vivo chemical mapping of the Methanosarcina acetivorans ribosome and its dimerization via a repurposed enzyme and translation factor.The Journal of biological chemistry · 2025Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be nearly universally conserved. Here we identify clades of archaea that have highly divergent ribosomal RNA sequences in the PTC. To understand how these PTC sequences fold, we determined cryo-EM structures of the 70S and 50S ribosomes to 2.4 Å and 2 Å, respectively, from the hyperthermophilic archaeon Pyrobaculum calidifontis. PTC sequence variation leads to the rearrangement of key base triples, and differences between archaeal and bacterial ribosomal proteins enable sequence variation in archaeal PTCs. Finally, we identify an archaeal ribosome hibernation factor, Dri, that differs from known bacterial and eukaryotic hibernation factors and is found in multiple archaeal phyla. Overall, this work identifies factors that regulate ribosome function in archaea and reveals a larger diversity of the most ancient sequences in the ribosome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.