Evidence map›Paper›PMID 28180299›Full record

ArticleNucleic acids research2017

Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA.

Sari Kassem, Zoltan Villanyi, Martine A Collart

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
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  4. Cotranslational assembly directs the biogenesis of the mProceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Regulation and outcomes of localized RNA translation.Wiley interdisciplinary reviews. RNA · 2022
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Sari KassemDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics Geneva, University of Geneva, Geneva, Switzerland
Zoltan VillanyiDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics Geneva, University of Geneva, Geneva, Switzerland
Martine A CollartDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics Geneva, University of Geneva, Geneva, Switzerland
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation of histones regulates gene expression in eukaryotes. In the yeast Saccharomyces cerevisiae it depends mainly upon the ADA and SAGA histone acetyltransferase complexes for which Gcn5 is the catalytic subunit. Previous screens have determined that global acetylation is reduced in cells lacking subunits of the Ccr4–Not complex, a global regulator of eukaryotic gene expression. In this study we have characterized the functional connection between the Ccr4–Not complex and SAGA. We show that SAGA mRNAs encoding a core set of SAGA subunits are tethered together for co-translational assembly of the encoded proteins. Ccr4–Not subunits bind SAGA mRNAs and promote the co-translational assembly of these subunits. This is needed for integrity of SAGA. In addition, we determine that a glycolytic enzyme, the glyceraldehyde-3-phosphate dehydrogenase Tdh3, a prototypical moonlighting protein, is tethered at this site of Ccr4–Not-dependent co-translational SAGA assembly and functions as a chaperone.

Indexed as

Gene Expression Regulation, FungalGenes, FungalGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Histone AcetyltransferasesModels, BiologicalMutationp300-CBP-Associated FactorProtein MultimerizationProtein SubunitsRibonucleasesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsADA2 protein, S cerevisiaeCCR4 protein, S cerevisiaeGCN5 protein, S cerevisiaeGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)Histone AcetyltransferasesNOT5 protein, S cerevisiaep300-CBP-Associated FactorProtein SubunitsRibonucleasesRNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSPT20 protein, S cerevisiaeTDH3 protein, S cerevisiaeTrans-ActivatorsTranscription Factors

Identifiers

PMID28180299
PMCPMC5388395
OpenAlexW2510524631

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.