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Evolutionary, structural and functional explorations of non-coding RNA and protein genetic robustness

Dorien S Coray, Nellie Sibaeva, Stephanie McGimpsey, View ORCID ProfilePaul P Gardner
doi: https://doi.org/10.1101/480087
Dorien S Coray
aSchool of Biological Sciences, University of Canterbury, Christchurch, NZ
bBiomolecular Interaction Centre, University of Canterbury, Christchurch, NZ
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Nellie Sibaeva
bBiomolecular Interaction Centre, University of Canterbury, Christchurch, NZ
cSchool of Biological Sciences, University of Auckland, NZ.
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Stephanie McGimpsey
aSchool of Biological Sciences, University of Canterbury, Christchurch, NZ
bBiomolecular Interaction Centre, University of Canterbury, Christchurch, NZ
dDepartment of Biochemistry, University of Otago, New Zealand
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Paul P Gardner
aSchool of Biological Sciences, University of Canterbury, Christchurch, NZ
bBiomolecular Interaction Centre, University of Canterbury, Christchurch, NZ
dDepartment of Biochemistry, University of Otago, New Zealand
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  • ORCID record for Paul P Gardner
  • For correspondence: paul.gardner@otago.ac.nz
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Abstract

The reactions of functional molecules like RNAs and proteins to mutation affect both host cell viability and biomolecular evolution. These molecules are considered robust if function is maintained alongside the mutation. RNAs and proteins have different structural and functional characteristics that affect their robustness, and to date, comparisons between them have been theoretical. In this work, we tested the relative mutational robustness of RNA and protein pairs using three approaches: evolutionary, structural, and functional. We compared the nucleotide diversities of functional RNAs with those of matched proteins. Across different levels of conservation, there were no differences in nucleotide-level variations between the biomolecules. We then directly tested the robustness of the RNA and protein pairs with in vitro and in silico mutagenesis of their respective genes. The in silico experiments showed that RNAs and proteins reacted similarly to point mutations and insertions or deletions. In vitro, mutated fluorescent RNAs retained greater levels of function than the proteins, but this may be because of differences in the robustness of the specific individual molecules rather than being indicative of a larger trend. In this first experimental comparison of proteins and RNAs, we found no consistent quantitative differences in mutational robustness. Future work on potential qualitative differences and other forms of robustness will give further insight into the evolution and functionality of biomolecules.

Significance Statement The ability of functional RNAs and proteins to maintain function despite mutations in their respective genes is known as mutational robustness. Robustness impacts how molecules maintain and change phenotypes, which has a bearing on the evolution and the origin of life as well as influences modern biotechnology. Both RNA and protein have mechanisms that allow them to absorb DNA-level changes. Proteins have a redundant genetic code and non-coding RNAs can maintain structure through flexible base-pairing possibilities. The few theoretical treatments comparing RNA and protein robustness differ in their conclusions. In this experimental comparison of RNAs and proteins, we find that RNAs and proteins achieve remarkably similar degrees of overall genetic robustness.

Footnotes

  • Abbreviations:

    BANP, CRISPR, Indels, ncRNA, ORF, RNase, RNP, rRNA, tRNA, RY

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted November 29, 2018.
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Evolutionary, structural and functional explorations of non-coding RNA and protein genetic robustness
Dorien S Coray, Nellie Sibaeva, Stephanie McGimpsey, Paul P Gardner
bioRxiv 480087; doi: https://doi.org/10.1101/480087
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Evolutionary, structural and functional explorations of non-coding RNA and protein genetic robustness
Dorien S Coray, Nellie Sibaeva, Stephanie McGimpsey, Paul P Gardner
bioRxiv 480087; doi: https://doi.org/10.1101/480087

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