Evidence map›Paper›PMID 34730946›Full record

ArticleACS synthetic biology2021

Broadening the Toolkit for Quantitatively Evaluating Noncanonical Amino Acid Incorporation in Yeast.

Jessica T Stieglitz, Kelly A Potts, James A Van Deventer

Abstract read
In one paragraph

Article in ACS synthetic biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed.

  1. Article
  2. BeyondChemical reviews · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Exploration ofACS synthetic biology · 2022
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Jessica T StieglitzChemical and Biological Engineering Department, Tufts University, Medford, Massachusetts 02155, United States.ORCID 0000-0003-3845-0712
Kelly A PottsChemical and Biological Engineering Department, Tufts University, Medford, Massachusetts 02155, United States.ORCID 0000-0002-0897-2803
James A Van DeventerChemical and Biological Engineering Department, Tufts University, Medford, Massachusetts 02155, United States.ORCID 0000-0003-4343-6157

Funding

The yeast surface as a platform for inhibitor discoveryR35GM133471 · NIGMS · TUFTS UNIVERSITY MEDFORD · PI James Allen Van Deventer · 2019 to 2026
$3.1M
NIGMS NIH HHS R35 GM133471
6 · The paper itself

Abstract

Genetic code expansion is a powerful approach for advancing critical fields such as biological therapeutic discovery. However, the machinery for genetically encoding noncanonical amino acids (ncAAs) is only available in limited plasmid formats, constraining potential applications. In extreme cases, the introduction of two separate plasmids, one containing an orthogonal translation system (OTS) to facilitate ncAA incorporation and a second for expressing a ncAA-containing protein of interest, is not possible due to a lack of the available selection markers. One strategy to circumvent this challenge is to express the OTS and protein of interest from a single vector. For what we believe is the first time in yeast, we describe here several sets of single plasmid systems (SPSs) for performing genetic code manipulation and compare the ncAA incorporation capabilities of these plasmids against the capabilities of previously described dual plasmid systems (DPSs). For both dual fluorescent protein reporters and yeast display reporters tested with multiple OTSs and ncAAs, measured ncAA incorporation efficiencies with SPSs were determined to be equal to efficiencies determined with DPSs. Click chemistry on yeast cells displaying ncAA-containing proteins was also shown to be feasible in both formats, although differences in reactivity between formats suggest the need for caution when using such approaches. Additionally, we investigated whether these reporters would support the separation of yeast strains known to exhibit distinct ncAA incorporation efficiencies. Model sorts conducted with mixtures of two strains transformed with the same SPS or DPS both led to the enrichment of a strain known to support a higher efficiency ncAA incorporation, suggesting that these reporters will be suitable for conducting screens for strains exhibiting enhanced ncAA incorporation efficiencies. Overall, our results confirm that SPSs are well behaved in yeast and provide a convenient alternative to DPSs. SPSs are expected to be invaluable for conducting high-throughput investigations of the effects of genetic or genomic changes on ncAA incorporation efficiency and, more fundamentally, the eukaryotic translation apparatus.

Indexed as

Amino AcidsAmino Acyl-tRNA SynthetasesCodon, TerminatorEvaluation Studies as TopicGenes, ReporterGenetic CodePlasmidsProtein BiosynthesisProtein EngineeringYeastsAmino AcidsAmino Acyl-tRNA SynthetasesCodon, Terminatoraminoacyl-tRNA synthetasegenetic code expansionnoncanonical amino acidsorthogonal translation systemsyeast display

Identifiers

PMID34730946
PMCPMC8936162

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.