Evidence map›Paper›PMID 27974378›Full record

ArticleEMBO reports2017

Architecture of the yeast Elongator complex.

Maria I Dauden, Jan Kosinski, Olga Kolaj-Robin, Ambroise Desfosses, Alessandro Ori, Celine Faux, Niklas A Hoffmann, Osita F Onuma, Karin D Breunig, Martin Beck and 4 more

Abstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

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  4. Microbiology spectrum · 2026
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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

14 authors.

Maria I DaudenEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Jan KosinskiEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Olga Kolaj-RobinUniversité de Strasbourg, IGBMC, Illkirch, France.
Ambroise DesfossesEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Alessandro OriEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Celine FauxUniversité de Strasbourg, IGBMC, Illkirch, France.
Niklas A HoffmannEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.
Osita F OnumaInstitute of Biology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Karin D BreunigInstitute of Biology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.ORCID 0000-0002-0319-3114
Martin BeckEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0002-7397-1321
Carsten SachseEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany.ORCID 0000-0002-1168-5143
Bertrand SéraphinUniversité de Strasbourg, IGBMC, Illkirch, France.
Sebastian GlattMax Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland sebastian.glatt@uj.edu.pl cmueller@embl.de.
Christoph W MüllerEuropean Molecular Biology Laboratory, Structural and Computational Biology Unit, Heidelberg, Germany sebastian.glatt@uj.edu.pl cmueller@embl.de.ORCID 0000-0003-2176-8337

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The highly conserved eukaryotic Elongator complex performs specific chemical modifications on wobble base uridines of tRNAs, which are essential for proteome stability and homeostasis. The complex is formed by six individual subunits (Elp1-6) that are all equally important for its tRNA modification activity. However, its overall architecture and the detailed reaction mechanism remain elusive. Here, we report the structures of the fully assembled yeast Elongator and the Elp123 sub-complex solved by an integrative structure determination approach showing that two copies of the Elp1, Elp2, and Elp3 subunits form a two-lobed scaffold, which binds Elp456 asymmetrically. Our topological models are consistent with previous studies on individual subunits and further validated by complementary biochemical analyses. Our study provides a structural framework on how the tRNA modification activity is carried out by Elongator.

Indexed as

Models, MolecularFungal ProteinsMultiprotein ComplexesMutationProtein BindingProtein ConformationProtein MultimerizationProtein SubunitsProtein TransportSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipFungal ProteinsMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiae Proteinselectron microscopyElongatorSaccharomyces cerevisiaetRNA modificationyeast

Identifiers

PMID27974378
PMCPMC5286394

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.