ArticleMolecular biology and evolution2018
Revising the Structural Diversity of Ribosomal Proteins Across the Three Domains of Life.
Article in Molecular biology and evolution, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- RiboScreenBiomedicines · 2026Review
- A family of ribosome hibernation factors widespread in Archaea.Nature communications · 2026Article
- Evolution of Translation Initiation Factor 2 Extensions Links Initiation to Bacterial Stress Response.bioRxiv : the preprint server for biology · 2026Article
- BRIX1 activated by mTORC1-SP1 signaling regulates ribosome biogenesis and alternative splicing to promote hepatocellular carcinoma progression.Hepatology international · 2026Article
- A symbiotic origin of the ribosome?PNAS nexus · 2026Article
- pH Sensitivity of the SERF1a Conformational Ensemble.ACS omega · 2026Article
- Latent Regulatory Programs Generate Synthetic T Cell States with Enhanced Therapeutic Potential.bioRxiv : the preprint server for biology · 2026Article
- Near-cognate tRNAs enhance tRNA rejection and prime the ribosome for rapid subsequent tRNA testing.Biophysical journal · 2025Article
- 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
- FTO degrader impairs ribosome biogenesis and protein translation in acute myeloid leukemia.Science advances · 2025Article
- Prognostic model identification of ribosome biogenesis-related genes in pancreatic cancer based on multiple machine learning analyses.Discover oncology · 2025Article
- Biallelic variants in the conserved ribosomal protein chaperone geneProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structures of Saccharolobus solfataricus initiation complexes with leaderless mRNAs highlight archaeal features and eukaryotic proximity.Nature communications · 2025Article
- Review
- Decoding the molecular script of 2'-O-ribomethylation: Implications across CNS disorders.Heliyon · 2024Review
- Single-Molecule Studies of Cognate and Near-Cognate Elongation in anbioRxiv : the preprint server for biology · 2024Article
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- RiboScreenInternational journal of molecular sciences · 2024Article
- Costs of ribosomal RNA stabilization affect ribosome composition at maximum growth rate.Communications biology · 2024Article
- Domain definition and preliminary functional exploration of the endonuclease NOBP-1 in Strongyloides stercoralis.Parasites & vectors · 2023Article
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Authors and funding
3 authors.
Funding
Abstract
Ribosomal proteins are indispensable components of a living cell, and yet their structures are remarkably diverse in different species. Here we use manually curated structural alignments to provide a comprehensive catalog of structural variations in homologous ribosomal proteins from bacteria, archaea, eukaryotes, and eukaryotic organelles. By resolving numerous ambiguities and errors of automated structural and sequence alignments, we uncover a whole new class of structural variations that reside within seemingly conserved segments of ribosomal proteins. We then illustrate that these variations reflect an apparent adaptation of ribosomal proteins to the specific environments and lifestyles of living species. Finally, we show that most of these structural variations reside within nonglobular extensions of ribosomal proteins-protein segments that are thought to promote ribosome biogenesis by stabilizing the proper folding of ribosomal RNA. We show that although the extensions are thought to be the most ancient peptides on our planet, they are in fact the most rapidly evolving and most structurally and functionally diverse segments of ribosomal proteins. Overall, our work illustrates that, despite being long considered as slowly evolving and highly conserved, ribosomal proteins are more complex and more specialized than is generally recognized.
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