Evidence map›Paper›PMID 31309145›Full record

ArticleScience advances2019

Molecular basis of tRNA recognition by the Elongator complex.

Maria I Dauden, Marcin Jaciuk, Felix Weis, Ting-Yu Lin, Carolin Kleindienst, Nour El Hana Abbassi, Heena Khatter, Rościsław Krutyhołowa, Karin D Breunig, Jan Kosinski and 2 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-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

36 citing papers in PubMed, 56 citations in OpenAlex.

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  4. Transcription Factors in Plant Gene Expression Regulation.International journal of molecular sciences · 2025
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  10. ELP3 stabilizes c-Myc to promote tumorigenesis.Journal of molecular cell biology · 2024
    Article
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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 3 institutions in 2 countries.

Maria I DaudenEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0003-2129-3941
Marcin JaciukMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland.ORCID 0000-0003-1251-1492
Felix WeisEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0002-8137-3532
Ting-Yu LinMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland.ORCID 0000-0001-7914-2164
Carolin KleindienstInstitute of Biology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.ORCID 0000-0003-0107-2199
Nour El Hana AbbassiMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland.ORCID 0000-0002-0385-7953
Heena KhatterEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0002-0915-6074
Rościsław KrutyhołowaMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland.ORCID 0000-0002-8200-5627
Karin D BreunigInstitute of Biology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.ORCID 0000-0002-0319-3114
Jan KosinskiEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0002-3641-0322
Christoph W MüllerEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0003-2176-8337
Sebastian GlattMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland.ORCID 0000-0003-2815-7133
European Molecular Biology Laboratory · DEJagiellonian University · PLMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The highly conserved Elongator complex modifies transfer RNAs (tRNAs) in their wobble base position, thereby regulating protein synthesis and ensuring proteome stability. The precise mechanisms of tRNA recognition and its modification reaction remain elusive. Here, we show cryo-electron microscopy structures of the catalytic subcomplex of Elongator and its tRNA-bound state at resolutions of 3.3 and 4.4 Å. The structures resolve details of the catalytic site, including the substrate tRNA, the iron-sulfur cluster, and a SAM molecule, which are all validated by mutational analyses in vitro and in vivo. tRNA binding induces conformational rearrangements, which precisely position the targeted anticodon base in the active site. Our results provide the molecular basis for substrate recognition of Elongator, essential to understand its cellular function and role in neurodegenerative diseases and cancer.

Indexed as

AnticodonBinding SitesCatalytic DomainHistone AcetyltransferasesModels, MolecularMolecular ConformationMultiprotein ComplexesPeptide Elongation FactorsProtein BindingRNA, TransferSaccharomyces cerevisiae ProteinsAnticodonHistone AcetyltransferasesIKI3 protein, S cerevisiaeMultiprotein ComplexesPeptide Elongation FactorsRNA, TransferSaccharomyces cerevisiae Proteins

Identifiers

PMID31309145
PMCPMC6620098
OpenAlexW2959627954

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.