Evidence map›Paper›PMID 32561742›Full record

ArticleNature communications2020

Substrate specificity of the TRAMP nuclear surveillance complexes.

Clémentine Delan-Forino, Christos Spanos, Juri Rappsilber, David Tollervey

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-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

24 citing papers in PubMed, 37 citations in OpenAlex.

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  8. TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

4 authors at 1 institution in 2 countries.

Clémentine Delan-ForinoWellcome Center for Cell Biology, University of Edinburgh, Kings Buildings, Swann Building, Edinburgh, EH9 3BF, UK.
Christos SpanosWellcome Center for Cell Biology, University of Edinburgh, Kings Buildings, Swann Building, Edinburgh, EH9 3BF, UK.ORCID http://orcid.org/0000-0002-4376-8242
Juri RappsilberWellcome Center for Cell Biology, University of Edinburgh, Kings Buildings, Swann Building, Edinburgh, EH9 3BF, UK.ORCID http://orcid.org/0000-0001-5999-1310
David TollerveyWellcome Center for Cell Biology, University of Edinburgh, Kings Buildings, Swann Building, Edinburgh, EH9 3BF, UK. D.Tollervey@ed.ac.uk.ORCID http://orcid.org/0000-0003-2894-2772
Wellcome Centre for Cell Biology · GB

Funding

Wellcome Trust 077248Wellcome Trust 103139Wellcome Trust 103139/Z/13/ZWellcome Trust 108504Wellcome Trust 203149
6 · The paper itself

Abstract

During nuclear surveillance in yeast, the RNA exosome functions together with the TRAMP complexes. These include the DEAH-box RNA helicase Mtr4 together with an RNA-binding protein (Air1 or Air2) and a poly(A) polymerase (Trf4 or Trf5). To better determine how RNA substrates are targeted, we analyzed protein and RNA interactions for TRAMP components. Mass spectrometry identified three distinct TRAMP complexes formed in vivo. These complexes preferentially assemble on different classes of transcripts. Unexpectedly, on many substrates, including pre-rRNAs and pre-mRNAs, binding specificity is apparently conferred by Trf4 and Trf5. Clustering of mRNAs by TRAMP association shows co-enrichment for mRNAs with functionally related products, supporting the significance of surveillance in regulating gene expression. We compared binding sites of TRAMP components with multiple nuclear RNA binding proteins, revealing preferential colocalization of subsets of factors. TRF5 deletion reduces Mtr4 recruitment and increases RNA abundance for mRNAs specifically showing high Trf5 binding.

Indexed as

Adaptor Proteins, Signal TransducingCell NucleusDEAD-box RNA HelicasesDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesExosome Multienzyme Ribonuclease ComplexMass SpectrometryMutationProtein Interaction MappingRNA, MessengerRNA PrecursorsRNA-SeqRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityAdaptor Proteins, Signal TransducingAir1 protein, S cerevisiaeAir2 protein, S cerevisiaeDEAD-box RNA HelicasesDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesExosome Multienzyme Ribonuclease ComplexMTR4 protein, S cerevisiaePAP2 protein, S cerevisiaeRNA, MessengerRNA PrecursorsSaccharomyces cerevisiae ProteinsTrf5 protein, S cerevisiae

Identifiers

PMID32561742
PMCPMC7305330
OpenAlexW3036207447

What OpenQuestion holds

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LicenceCC BY
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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.