Evidence map›Paper›PMID 24047896›Full record

ArticleThe Journal of biological chemistry2013

Cotranscriptional recruitment of RNA exosome cofactors Rrp47p and Mpp6p and two distinct Trf-Air-Mtr4 polyadenylation (TRAMP) complexes assists the exonuclease Rrp6p in the targeting and degradation of an aberrant messenger ribonucleoprotein particle (mRNP) in yeast.

Igor Stuparevic, Christine Mosrin-Huaman, Nadège Hervouet-Coste, Mateja Remenaric, A Rachid Rahmouni

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.5field-weighted citation impact, top 18% 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, 35 citations in OpenAlex.

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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 2 institutions in 1 country.

Igor StuparevicFrom the Centre de Biophysique Moléculaire, Unité Propre de Recherche (UPR) 4301 du CNRS, rue Charles Sadron, 45071 Orléans, France.
Christine Mosrin-Huaman
Nadège Hervouet-Coste
Mateja Remenaric
A Rachid Rahmouni
Centre National de la Recherche Scientifique · FRCentre de Biophysique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cotranscriptional mRNA processing and packaging reactions that lead to the formation of export-competent messenger ribonucleoprotein particles (mRNPs) are under the surveillance of quality control steps. Aberrant mRNPs resulting from faulty events are retained in the nucleus with ensuing elimination of their mRNA component. The molecular mechanisms by which the surveillance system recognizes defective mRNPs and stimulates their destruction by the RNA degradation machinery are still not completely elucidated. Using an experimental approach in which mRNP formation in yeast is disturbed by the action of the bacterial Rho helicase, we have shown previously that the targeting of Rho-induced aberrant mRNPs is mediated by Rrp6p, which is recruited cotranscriptionally in association with Nrd1p following Rho action. Here we investigated the specific involvement in this quality control process of different cofactors associated with the nuclear RNA degradation machinery. We show that, in addition to the main hydrolytic action of the exonuclease Rrp6p, the cofactors Rrp47p, Mpp6p as well as the Trf-Air-Mtr4 polyadenylation (TRAMP) components Trf4p, Trf5p, and Air2p contribute significantly by stimulating the degradation process upon their cotranscriptional recruitment. Trf4p and Trf5p are apparently recruited in two distinct TRAMP complexes that both contain Air2p as component. Surprisingly, Rrp47p appears to play an important role in mutual protein stabilization with Rrp6p, which highlights a close association between the two partners. Together, our results provide an integrated view of how different cofactors of the RNA degradation machinery cooperate to target and eliminate aberrant mRNPs.

Indexed as

Adaptor Proteins, Signal TransducingDEAD-box RNA HelicasesDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesEnzyme StabilityExosome Multienzyme Ribonuclease ComplexMultienzyme ComplexesNuclear ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingAir2 protein, S cerevisiaeDEAD-box RNA HelicasesDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesExosome Multienzyme Ribonuclease ComplexLRP1 protein, S cerevisiaemessenger ribonucleoproteinMpp6 protein, S cerevisiaeMTR4 protein, S cerevisiaeMultienzyme ComplexesNuclear ProteinsPAP2 protein, S cerevisiaeRibonucleoproteinsRNA-Binding ProteinsRNA, FungalRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTrf5 protein, S cerevisiaemRNAmRNA DecayRNARNA MetabolismRNA Processing

Identifiers

PMID24047896
PMCPMC3814775
OpenAlexW2004443873

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.