Evidence map›Paper›PMID 36617428›Full record

ArticleNucleic acids research2023

Cryo-EM structure of the fully assembled Elongator complex.

Marcin Jaciuk, David Scherf, Karol Kaszuba, Monika Gaik, Alexander Rau, Anna Kościelniak, Rościsław Krutyhołowa, Michał Rawski, Paulina Indyka, Andrea Graziadei and 10 more

Open access · goldFull text 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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
9.7field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. An Orthogonal Way of Writing the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Loss of both wobbleUFrontiers in plant science · 2025
    Article
  14. The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Biomolecules · 2023
    Article
  20. 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

20 authors at 5 institutions in 3 countries.

Marcin JaciukMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
David ScherfInstitute for Biology, Department for Microbiology, University of Kassel, Kassel 34132, Germany.
Karol KaszubaEuropean Molecular Biology Laboratory Hamburg, Hamburg 22607, Germany.
Monika GaikMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.ORCID 0000-0003-4939-3821
Alexander RauBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin 13355, Germany.
Anna KościelniakMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Rościsław KrutyhołowaMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Michał RawskiMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Paulina IndykaMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Andrea GraziadeiBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin 13355, Germany.
Andrzej Chramiec-GłąbikMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Anna BielaMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Dominika DoboszMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Ting-Yu LinMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Nour-El-Hana AbbassiMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Alexander HammermeisterMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.
Juri RappsilberBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin 13355, Germany.ORCID 0000-0001-5999-1310
Jan KosinskiEuropean Molecular Biology Laboratory Hamburg, Hamburg 22607, Germany.ORCID 0000-0002-3641-0322
Raffael SchaffrathInstitute for Biology, Department for Microbiology, University of Kassel, Kassel 34132, Germany.ORCID 0000-0001-9484-5247
Sebastian GlattMalopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow 30-387, Poland.ORCID 0000-0003-2815-7133
Jagiellonian University · PLUniversity of Kassel · DEEuropean Molecular Biology Laboratory · DETechnische Universität Berlin · DEWellcome Centre for Cell Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transfer RNA (tRNA) molecules are essential to decode messenger RNA codons during protein synthesis. All known tRNAs are heavily modified at multiple positions through post-transcriptional addition of chemical groups. Modifications in the tRNA anticodons are directly influencing ribosome decoding and dynamics during translation elongation and are crucial for maintaining proteome integrity. In eukaryotes, wobble uridines are modified by Elongator, a large and highly conserved macromolecular complex. Elongator consists of two subcomplexes, namely Elp123 containing the enzymatically active Elp3 subunit and the associated Elp456 hetero-hexamer. The structure of the fully assembled complex and the function of the Elp456 subcomplex have remained elusive. Here, we show the cryo-electron microscopy structure of yeast Elongator at an overall resolution of 4.3 Å. We validate the obtained structure by complementary mutational analyses in vitro and in vivo. In addition, we determined various structures of the murine Elongator complex, including the fully assembled mouse Elongator complex at 5.9 Å resolution. Our results confirm the structural conservation of Elongator and its intermediates among eukaryotes. Furthermore, we complement our analyses with the biochemical characterization of the assembled human Elongator. Our results provide the molecular basis for the assembly of Elongator and its tRNA modification activity in eukaryotes.

Indexed as

Multiprotein ComplexesPeptide Chain Elongation, TranslationalRNA-Binding ProteinsSaccharomyces cerevisiaeAnimalsCryoelectron MicroscopyHistone AcetyltransferasesHumansMiceProtein BindingRNA, TransferSaccharomyces cerevisiae ProteinsHistone AcetyltransferasesMultiprotein ComplexesRNA-Binding ProteinsRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID36617428
PMCPMC10018365
OpenAlexW4313799967

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read146
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.