ArticleNucleic acids research2025
Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A conserved archaeal protein with evolutionary links to bacterial ribosome hibernation and eukaryotic energy sensing.The EMBO journal · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.Nature communications · 2026Article
- A family of ribosome hibernation factors widespread in Archaea.Nature communications · 2026Article
- A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.bioRxiv : the preprint server for biology · 2026Article
- 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
- Structure of an archaeal ribosome reveals a divergent active site and hibernation factor.Nature microbiology · 2025Article
- Spatial regulation of ribosomal protein gene expression revealed by spatial transcriptomic analysis in the water fernFrontiers in plant science · 2025Article
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7 authors.
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Abstract
Protein synthesis (translation) consumes a substantial proportion of cellular resources, prompting specialized mechanisms to reduce translation under adverse conditions. Ribosome inactivation often involves ribosome-interacting proteins. In both bacteria and eukaryotes, various ribosome-interacting proteins facilitate ribosome dimerization or hibernation, and/or prevent ribosomal subunits from associating, enabling the organisms to adapt to stress. Despite extensive studies on bacteria and eukaryotes, understanding factor-mediated ribosome dimerization or anti-association in archaea remains elusive. Here, we present cryo-electron microscopy structures of an archaeal 30S dimer complexed with an archaeal ribosome dimerization factor (designated aRDF), from Pyrococcus furiosus, resolved at a resolution of 3.2 Å. The complex features two 30S subunits stabilized by aRDF homodimers in a unique head-to-body architecture, which differs from the disome architecture observed during hibernation in bacteria and eukaryotes. aRDF interacts directly with eS32 ribosomal protein, which is essential for subunit association. The binding mode of aRDF elucidates its anti-association properties, which prevent the assembly of archaeal 70S ribosomes.
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