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Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae
by
Villén, Judit
, Ruiz, Bianca Y.
, Zhu, Yanrui
, Berg, Matthew D.
, Genereaux, Julie
, Allan, Tyler
, Rodriguez-Mias, Ricard A.
, Bahcheli, Alexander
, Brandl, Christopher J.
in
Investigations
2019
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![Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae](https://www.mbrl.ae/o/mbrl-theme/images/site-assets/generic/no-book-image.png)
Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae
by
Villén, Judit
, Ruiz, Bianca Y.
, Zhu, Yanrui
, Berg, Matthew D.
, Genereaux, Julie
, Allan, Tyler
, Rodriguez-Mias, Ricard A.
, Bahcheli, Alexander
, Brandl, Christopher J.
in
Investigations
2019
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Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae
![Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae](https://syndetics.com/index.aspx?isbn=/mc.gif&issn=0016-6731&client=MBRL&type=mbrl)
Journal Article
Modulating Mistranslation Potential of tRNASer in Saccharomyces cerevisiae
2019
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Overview
Mistranslation, incorporating an amino acid not specified by the “standard” genetic code, has applications in research and synthetic biology. Since mistranslation is toxic, its level must be modulated. Using a serine tRNA with a proline anticodon, we identify...
Transfer RNAs (tRNAs) read the genetic code, translating nucleic acid sequence into protein. For tRNA
Ser
the anticodon does not specify its aminoacylation. For this reason, mutations in the tRNA
Ser
anticodon can result in amino acid substitutions, a process called mistranslation. Previously, we found that tRNA
Ser
with a proline anticodon was lethal to cells. However, by incorporating secondary mutations into the tRNA, mistranslation was dampened to a nonlethal level. The goal of this work was to identify second-site substitutions in tRNA
Ser
that modulate mistranslation to different levels. Targeted changes to putative identity elements led to total loss of tRNA function or significantly impaired cell growth. However, through genetic selection, we identified 22 substitutions that allow nontoxic mistranslation. These secondary mutations are primarily in single-stranded regions or substitute G:U base pairs for Watson–Crick pairs. Many of the variants are more toxic at low temperature and upon impairing the rapid tRNA decay pathway. We suggest that the majority of the secondary mutations affect the stability of the tRNA in cells. The temperature sensitivity of the tRNAs allows conditional mistranslation. Proteomic analysis demonstrated that tRNA
Ser
variants mistranslate to different extents with diminished growth correlating with increased mistranslation. When combined with a secondary mutation, other anticodon substitutions allow serine mistranslation at additional nonserine codons. These mistranslating tRNAs have applications in synthetic biology, by creating “statistical proteins,” which may display a wider range of activities or substrate specificities than the homogenous form.
Publisher
Genetics Society of America
Subject
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