Evidence map›Paper›PMID 27872205›Full record

ArticleEMBO reports2017

Molecular architecture of the yeast Elongator complex reveals an unexpected asymmetric subunit arrangement.

Dheva T Setiaputra, Derrick Th Cheng, Shan Lu, Jesse M Hansen, Udit Dalwadi, Cindy Hy Lam, Jeffrey L To, Meng-Qiu Dong, Calvin K Yip

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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Microbiology spectrum · 2026
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  12. How Elongator Acetylates tRNA Bases.International journal of molecular sciences · 2020
    Review
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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

9 authors.

Dheva T SetiaputraDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Derrick Th ChengDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Shan LuNational Institute of Biological Sciences, Beijing, Beijing, China.
Jesse M HansenDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Udit DalwadiDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Cindy Hy LamDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Jeffrey L ToDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, Beijing, China.
Calvin K YipDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada calvin.yip@ubc.ca.ORCID 0000-0003-1779-9501

Funding

CIHR
6 · The paper itself

Abstract

Elongator is a ~850 kDa protein complex involved in multiple processes from transcription to tRNA modification. Conserved from yeast to humans, Elongator is assembled from two copies of six unique subunits (Elp1 to Elp6). Despite the wealth of structural data on the individual subunits, the overall architecture and subunit organization of the full Elongator and the molecular mechanisms of how it exerts its multiple activities remain unclear. Using single-particle electron microscopy (EM), we revealed that yeast Elongator adopts a bilobal architecture and an unexpected asymmetric subunit arrangement resulting from the hexameric Elp456 subassembly anchored to one of the two Elp123 lobes that form the structural scaffold. By integrating the EM data with available subunit crystal structures and restraints generated from cross-linking coupled to mass spectrometry, we constructed a multiscale molecular model that showed the two Elp3, the main catalytic subunit, are located in two distinct environments. This work provides the first structural insights into Elongator and a framework to understand the molecular basis of its multifunctionality.

Indexed as

Models, MolecularConserved SequenceEvolution, MolecularFungal ProteinsHistone AcetyltransferasesMass SpectrometryMultiprotein ComplexesProtein BindingProtein ConformationProtein MultimerizationProtein SubunitsSaccharomyces cerevisiae ProteinsSequence DeletionStructure-Activity RelationshipFungal ProteinsHistone AcetyltransferasesMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiae Proteinselectron microscopyElongatorstructuretRNA modification

Identifiers

PMID27872205
PMCPMC5286391

What OpenQuestion holds

Textmetadata
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.