Evidence map›Paper›PMID 31748520›Full record

ArticleNature communications2019

Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes in yeast.

Alberto Elías-Villalobos, Damien Toullec, Céline Faux, Martial Séveno, Dominique Helmlinger

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

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  16. Structure of the human SAGA coactivator complex.Nature structural & molecular biology · 2021
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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

5 authors at 1 institution in 1 country.

Alberto Elías-VillalobosCRBM, CNRS, University of Montpellier, Montpellier, France.ORCID http://orcid.org/0000-0001-8299-2063
Damien ToullecCRBM, CNRS, University of Montpellier, Montpellier, France.
Céline FauxCRBM, CNRS, University of Montpellier, Montpellier, France.
Martial SévenoBioCampus Montpellier, CNRS, INSERM, University of Montpellier, Montpellier, France.
Dominique HelmlingerCRBM, CNRS, University of Montpellier, Montpellier, France. dhelmlinger@crbm.cnrs.fr.ORCID http://orcid.org/0000-0003-1501-0423
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription initiation involves the coordinated activities of large multimeric complexes, but little is known about their biogenesis. Here we report several principles underlying the assembly and topological organization of the highly conserved SAGA and NuA4 co-activator complexes, which share the Tra1 subunit. We show that Tra1 contributes to the overall integrity of NuA4, whereas, within SAGA, it specifically controls the incorporation of the de-ubiquitination module (DUB), as part of an ordered assembly pathway. Biochemical and functional analyses reveal the mechanism by which Tra1 specifically interacts with either SAGA or NuA4. Finally, we demonstrate that Hsp90 and its cochaperone TTT promote Tra1 de novo incorporation into both complexes, indicating that Tra1, the sole pseudokinase of the PIKK family, shares a dedicated chaperone machinery with its cognate kinases. Overall, our work brings mechanistic insights into the assembly of transcriptional complexes and reveals the contribution of dedicated chaperones to this process.

Indexed as

Gene Expression Regulation, FungalHistone AcetyltransferasesHSP90 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTrans-ActivatorsTranscription, GeneticHistone AcetyltransferasesHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMolecular ChaperonesNuA4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSchizosaccharomyces pombe ProteinsTRA1 protein, S cerevisiaeTrans-Activators

Identifiers

PMID31748520
PMCPMC6868236
OpenAlexW2989632299

What OpenQuestion holds

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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.