ReviewInternational journal of molecular sciences2009
The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly.
Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- An atlas of RNA-dependent proteins in cell division reveals the riboregulation of mitotic protein-protein interactions.Nature communications · 2025Article
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- Review
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- The RNA-Binding Function of Ribosomal Proteins and Ribosome Biogenesis Factors in Human Health and Disease.Biomedicines · 2023Review
- Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022Review
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Spatially Enriched Paralog Rearrangements Argue Functionally Diverse Ribosomes Arise during Cold Acclimation in Arabidopsis.International journal of molecular sciences · 2021Article
- Evolution of ribosomal protein network architectures.Scientific reports · 2021Article
- The role of disorder in RNA binding affinity and specificity.Open biology · 2020Article
- Clusters of bacterial RNA polymerase are biomolecular condensates that assemble through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- Dissecting macromolecular recognition sites in ribosome: implication to its self-assembly.RNA biology · 2019Article
- Nervous-Like Circuits in the Ribosome Facts, Hypotheses and Perspectives.International journal of molecular sciences · 2019Review
- Overexpressed L20 Rescues 50S Ribosomal Subunit Assembly Defects ofFrontiers in microbiology · 2019Article
- Revising the Structural Diversity of Ribosomal Proteins Across the Three Domains of Life.Molecular biology and evolution · 2018Article
- The mitochondrial ribosomal protein L13 is critical for the structural and functional integrity of the mitochondrion inThe Journal of biological chemistry · 2018Article
- BIS2Analyzer: a server for co-evolution analysis of conserved protein families.Nucleic acids research · 2017Article
- A structural perspective of RNA recognition by intrinsically disordered proteins.Cellular and molecular life sciences : CMLS · 2016Review
- The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits.Nucleic acids research · 2016Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Although during the past decade research has shown the functional importance of disorder in proteins, many of the structural and dynamics properties of intrinsically unstructured proteins (IUPs) remain to be elucidated. This review is focused on the role of the extensions of the ribosomal proteins in the early steps of the assembly of the eubacterial 50 S subunit. The recent crystallographic structures of the ribosomal particles have revealed the picture of a complex assembly pathway that condenses the rRNA and the ribosomal proteins into active ribosomes. However, little is know about the molecular mechanisms of this process. It is thought that the long basic r-protein extensions that penetrate deeply into the subunit cores play a key role through disorder-order transitions and/or co-folding mechanisms. A current view is that such structural transitions may facilitate the proper rRNA folding. In this paper, the structures of the proteins L3, L4, L13, L20, L22 and L24 that have been experimentally found to be essential for the first steps of ribosome assembly have been compared. On the basis of their structural and dynamics properties, three categories of extensions have been identified. Each of them seems to play a distinct function. Among them, only the coil-helix transition that occurs in a phylogenetically conserved cluster of basic residues of the L20 extension appears to be strictly required for the large subunit assembly in eubacteria. The role of alpha helix-coil transitions in 23 S RNA folding is discussed in the light of the calcium binding protein calmodulin that shares many structural and dynamics properties with L20.
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