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Sökning: WFRF:(Uversky Vladimir N.) > A conserved ribosom...

A conserved ribosomal protein has entirely dissimilar structures in different organisms

Schierholz, Léon (författare)
Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Umeå Centre for Microbial Research (UCMR)
Brown, Charlotte R. (författare)
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom
Helena-Bueno, Karla (författare)
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom
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Uversky, Vladimir N. (författare)
Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, FL, Tampa, United States
Hirt, Robert P. (författare)
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom
Barandun, Jonas (författare)
Umeå universitet,Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)
Melnikov, Sergey V. (författare)
Biosciences Institute, Newcastle University School of Medicine, Newcastle upon Tyne, United Kingdom
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 (creator_code:org_t)
Oxford University Press, 2024
2024
Engelska.
Ingår i: Molecular biology and evolution. - : Oxford University Press. - 0737-4038 .- 1537-1719. ; 41:1
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)

Nyckelord

fold-switching protein
microsporidia
ribosomal protein
ribosome evolution

Publikations- och innehållstyp

ref (ämneskategori)
art (ämneskategori)

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