Evidence map›Paper›PMID 29273753›Full record

ArticleNature communications2017

Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid.

Youngzee Song, Huihao Zhou, My-Nuong Vo, Yi Shi, Mir Hussain Nawaz, Oscar Vargas-Rodriguez, Jolene K Diedrich, John R Yates, Shuji Kishi, Karin Musier-Forsyth and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 9% of its field
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

29 citing papers in PubMed, 61 citations in OpenAlex.

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  18. CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. HumanThe Journal of biological chemistry · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 3 countries.

Youngzee SongThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA.
Huihao ZhouThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA.
My-Nuong VoThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA.
Yi ShiThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA.
Mir Hussain NawazThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA.
Oscar Vargas-RodriguezDepartment of Chemistry and Biochemistry, Center for RNA Biology, The Ohio State University, Columbus, OH, 43220, USA.
Jolene K DiedrichDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, USA.
John R YatesDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0001-5267-1672
Shuji KishiThe Scripps Laboratories for tRNA Synthetase Research and Department of Molecular Medicine, The Scripps Research Institute, Jupiter, FL, 33458, USA.
Karin Musier-ForsythDepartment of Chemistry and Biochemistry, Center for RNA Biology, The Ohio State University, Columbus, OH, 43220, USA.
Paul SchimmelThe Scripps Laboratories for tRNA Synthetase Research and the Department of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 92037, La Jolla, CA, USA. schimmel@scripps.edu.
Scripps Research Institute · USThe Ohio State University · USNew York University Abu Dhabi · AE

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
GENETIC APPROACHES TO PROTEIN/NUCLEIC ACID INTERACTIONSR01GM023562 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2012
$4.9M
Translational quality control by trans-editing domainsR01GM113656 · NIGMS · OHIO STATE UNIVERSITY · PI MUSIER-FORSYTH, KARIN M · 2015 to 2018
$1.1M
NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM023562NIGMS NIH HHS R01 GM113656
6 · The paper itself

Abstract

Hundreds of non-proteinogenic (np) amino acids (AA) are found in plants and can in principle enter human protein synthesis through foods. While aminoacyl-tRNA synthetase (AARS) editing potentially provides a mechanism to reject np AAs, some have pathological associations. Co-crystal structures show that vegetable-sourced azetidine-2-carboxylic acid (Aze), a dual mimic of proline and alanine, is activated by both human prolyl- and alanyl-tRNA synthetases. However, it inserts into proteins as proline, with toxic consequences in vivo. Thus, dual mimicry increases odds for mistranslation through evasion of one but not both tRNA synthetase editing systems.

Indexed as

Cell DeathMolecular MimicryAlanineAlanine-tRNA LigaseAmino AcidsAmino Acyl-tRNA SynthetasesAzetidinecarboxylic AcidHeLa CellsHumansProlineProtein BiosynthesisRNA EditingRNA, TransferVegetablesAlanineAlanine-tRNA LigaseAmino AcidsAmino Acyl-tRNA SynthetasesAzetidinecarboxylic AcidProlineprolyl T RNA synthetaseRNA, Transfer

Identifiers

PMID29273753
PMCPMC5741666
OpenAlexW2779188236

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.