Evidence map›Paper›PMID 37638745›Full record

ArticleNucleic acids research2023

Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase.

Bastiaan de Potter, Ingrid Vallee, Noelia Camacho, Luís Filipe Costa Póvoas, Aureliano Bonsembiante, Alba Pons I Pons, Ulrich Eckhard, Francesc-Xavier Gomis-Rüth, Xiang-Lei Yang, Paul Schimmel and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Review
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

12 authors at 5 institutions in 3 countries.

Bastiaan de PotterInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.ORCID 0000-0003-4479-2460
Ingrid ValleeThe Scripps Research Institute, Department of Molecular Medicine La Jolla, CA, USA.
Noelia CamachoInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.
Luís Filipe Costa PóvoasInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.
Aureliano BonsembianteInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.
Alba Pons I PonsInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.
Ulrich EckhardMolecular Biology Institute of Barcelona, Department of Structural Biology, Barcelona, Catalunya, Spain.
Francesc-Xavier Gomis-RüthMolecular Biology Institute of Barcelona, Department of Structural Biology, Barcelona, Catalunya, Spain.
Xiang-Lei YangThe Scripps Research Institute, Department of Molecular Medicine La Jolla, CA, USA.ORCID 0000-0003-4315-0204
Paul SchimmelThe Scripps Research Institute, Department of Molecular Medicine La Jolla, CA, USA.ORCID 0000-0002-0448-022X
Bernhard KuhleThe Scripps Research Institute, Department of Molecular Medicine La Jolla, CA, USA.
Lluís Ribas de PouplanaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Catalonia, Spain.ORCID 0000-0002-2087-0359
Institute for Research in Biomedicine · ESScripps Research Institute · USInstitut de Biologia Molecular de Barcelona · ESInstitució Catalana de Recerca i Estudis Avançats · ESUtrecht University · NL

Funding

Link extracellular function of tRNA synthetase with pathological mechanism of diseaseR35GM139627 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YANG, XIANG-LEI · 2021 to 2025
$2.3M
NIGMS NIH HHS R35 GM139627
6 · The paper itself

Abstract

Through their aminoacylation reactions, aminoacyl tRNA-synthetases (aaRS) establish the rules of the genetic code throughout all of nature. During their long evolution in eukaryotes, additional domains and splice variants were added to what is commonly a homodimeric or monomeric structure. These changes confer orthogonal functions in cellular activities that have recently been uncovered. An unusual exception to the familiar architecture of aaRSs is the heterodimeric metazoan mitochondrial SerRS. In contrast to domain additions or alternative splicing, here we show that heterodimeric metazoan mitochondrial SerRS arose from its homodimeric ancestor not by domain additions, but rather by collapse of an entire domain (in one subunit) and an active site ablation (in the other). The collapse/ablation retains aminoacylation activity while creating a new surface, which is necessary for its orthogonal function. The results highlight a new paradigm for repurposing a member of the ancient tRNA synthetase family.

Indexed as

Serine-tRNA LigaseAmino Acyl-tRNA SynthetasesAnimalsCatalytic DomainAmino Acyl-tRNA SynthetasesSerine-tRNA Ligase

Identifiers

PMID37638745
PMCPMC10570016
OpenAlexW4386209295

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.