Cited by 14RNA and protein synthesis mechanismsEvolution and Genetic DynamicsOrigins and Evolution of Life

In vivo selection of functional ribosomes with variations in the rRNA-binding site of Escherichia coli ribosomal protein S8: Evolutionary implications

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Moine, Hervé, Squires, Catherine L., Ehresmann, Bernard, Ehresmann, Chantal·2000·Proceedings of the National Academy of Sciences

Abstract

The highly conserved nature of rRNA sequences throughout evolution allows these molecules to be used to build philogenic trees of different species. It is unknown whether the stability of specific interactions and structural features of rRNA reflects an optimal adaptation to a functional task or an evolutionary trap. In the work reported here, we have applied an in vivo selection strategy to demonstrate that unnatural sequences do work as a functional replacement of the highly conserved binding site of ribosomal protein S8. However, growth competition experiments performed between Escherichia coli isolates containing natural and unnatural S8-binding sites showed that the fate of each isolate depended on the growth condition. In exponentially growing cells, one unnatural variant was found to be equivalent to wild type in competition experiments performed in rich media. In culture conditions leading to slow growth, however, cells containing the wild-type sequence were the ultimate winner of the competition, emphasizing that the wild-type sequence is, in fact, the most fit solution for the S8-binding site.

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  • The changes added by human players tend to agree with the 16S structural model, especially in regions linked to important functional sites, such as S8 and S15 binding sites, and a region that undergoes conformational readjustment during 30S assembly.

    “In Fig. 4, we show that the changes added by human players tend to agree with the 16S structural model, especially in regions linked to important functional sites, such as S8 and S15 binding sites, and a region that undergoes conformational readjustment during 30S assembly44–49.”

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References 29 · Cited by 14

Research works printed but not linked: 5

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Authors
Moine, H., Squires, C. L., Ehresmann, B., & Ehresmann, C.
Affiliations
Tufts University (US)
Venue
Proceedings of the National Academy of Sciences
Published
2000-01-18
Volume
97
Issue
2
Pages
605-610
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2099560457
Cited by
14
References
29
Citations by year
2024: 1 · 2018: 1 · 2014: 1 · 2013: 2 · 2012: 1
FWCI
0.36
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Brown University
  • National Institutes of Health
  • National Institute of General Medical Sciences (R01GM024751, GM24751)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
  • Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
Keywords
ribosomal protein S8, in vivo selection, Escherichia coli, ribosome function, growth competition, fitness, rRNA evolution, ribosome stability
MeSH terms
Spectinomycin, Base Sequence, Binding Sites, Binding, Competitive, Cell Division, Cloning, Molecular, Drug Resistance, Microbial, Escherichia coli, Protein Binding, Recombinant Fusion Proteins, Ribosomal Proteins, Ribosomes, RNA, Ribosomal, RNA, Ribosomal, 16S, Genetic Variation, Evolution, Molecular

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