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A conserved ribosomal protein has entirely dissimilar structures in different organisms
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom.
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom.
Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, FL, Tampa, United States.
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2024 (English)In: Molecular biology and evolution, ISSN 0737-4038, E-ISSN 1537-1719, Vol. 41, no 1, article id msad254Article in journal (Refereed) Published
Abstract [en]

Ribosomes from different species can markedly differ in their composition by including dozens of ribosomal proteins that are unique to specific lineages but absent in others. However, it remains unknown how ribosomes acquire new proteins throughout evolution. Here, to help answer this question, we describe the evolution of the ribosomal protein msL1/msL2 that was recently found in ribosomes from the parasitic microorganism clade, microsporidia. We show that this protein has a conserved location in the ribosome but entirely dissimilar structures in different organisms: in each of the analyzed species, msL1/msL2 exhibits an altered secondary structure, an inverted orientation of the N-Termini and C-Termini on the ribosomal binding surface, and a completely transformed 3D fold. We then show that this fold switching is likely caused by changes in the ribosomal msL1/msL2-binding site, specifically, by variations in rRNA. These observations allow us to infer an evolutionary scenario in which a small, positively charged, de novo-born unfolded protein was first captured by rRNA to become part of the ribosome and subsequently underwent complete fold switching to optimize its binding to its evolving ribosomal binding site. Overall, our work provides a striking example of how a protein can switch its fold in the context of a complex biological assembly, while retaining its specificity for its molecular partner. This finding will help us better understand the origin and evolution of new protein components of complex molecular assemblies-thereby enhancing our ability to engineer biological molecules, identify protein homologs, and peer into the history of life on Earth.

Place, publisher, year, edition, pages
Oxford University Press, 2024. Vol. 41, no 1, article id msad254
Keywords [en]
fold-switching protein, microsporidia, ribosomal protein, ribosome evolution
National Category
Biochemistry and Molecular Biology Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-219828DOI: 10.1093/molbev/msad254PubMedID: 37987564Scopus ID: 2-s2.0-85182091228OAI: oai:DiVA.org:umu-219828DiVA, id: diva2:1830110
Funder
Swedish Research Council, 2019-02011EU, Horizon 2020, 895166Available from: 2024-01-22 Created: 2024-01-22 Last updated: 2024-01-22Bibliographically approved

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Schierholz, LéonBarandun, Jonas

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