Evidence map›Paper›PMID 22683267›Full record

ArticleMolecular cell2012

Rrp6p controls mRNA poly(A) tail length and its decoration with poly(A) binding proteins.

Manfred Schmid, Mathias Bach Poulsen, Pawel Olszewski, Vicent Pelechano, Cyril Saguez, Ishaan Gupta, Lars M Steinmetz, Claire Moore, Torben Heick Jensen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  6. Article
  7. Article
  8. Substrate selectivity by the exonuclease Rrp6p.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Review
  11. The multitasking polyA tail: nuclear RNA maturation, degradation and export.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  12. Controlling nuclear RNA levels.Nature reviews. Genetics · 2018
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
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  20. Review
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 at 3 institutions in 3 countries.

Manfred SchmidCentre for mRNP Biogenesis and Metabolism, Department of Molecular Biology and Genetics, Aarhus University, C.F. Møllers Alle 3, Building 1130, DK-8000 Aarhus C., Denmark.
Mathias Bach Poulsen
Pawel Olszewski
Vicent Pelechano
Cyril Saguez
Ishaan Gupta
Lars M Steinmetz
Claire Moore
Torben Heick Jensen
Aarhus University · DKEuropean Molecular Biology Organization · DETufts University · US

Funding

Quantitative Trait Dissection by Reciprocal HemizygosityR01GM068717 · NIGMS · STANFORD UNIVERSITY · PI DAVIS, RONALD WAYNE · 2003 to 2014
$6.5M
Molecular mechanism of mRNA 3'-end formation in yeastR01GM041752 · NIGMS · TUFTS UNIVERSITY BOSTON · PI MOORE, CLAIRE L · 1989 to 2010
$4.0M
NIGMS NIH HHS GM041752NIGMS NIH HHS GM068717NIGMS NIH HHS R01 GM041752
6 · The paper itself

Abstract

Poly(A) (pA) tail binding proteins (PABPs) control mRNA polyadenylation, stability, and translation. In a purified system, S. cerevisiae PABPs, Pab1p and Nab2p, are individually sufficient to provide normal pA tail length. However, it is unknown how this occurs in more complex environments. Here we find that the nuclear exosome subunit Rrp6p counteracts the in vitro and in vivo extension of mature pA tails by the noncanonical pA polymerase Trf4p. Moreover, PABP loading onto nascent pA tails is controlled by Rrp6p; while Pab1p is the major PABP, Nab2p only associates in the absence of Rrp6p. This is because Rrp6p can interact with Nab2p and displace it from pA tails, potentially leading to RNA turnover, as evidenced for certain pre-mRNAs. We suggest that a nuclear mRNP surveillance step involves targeting of Rrp6p by Nab2p-bound pA-tailed RNPs and that pre-mRNA abundance is regulated at this level.

Indexed as

Base SequenceCell NucleusCytoplasmDNA-Directed DNA PolymeraseExoribonucleasesExosome Multienzyme Ribonuclease ComplexExosomesGene Expression Regulation, FungalModels, BiologicalMolecular Sequence DataNucleocytoplasmic Transport ProteinsOligonucleotide Array Sequence AnalysisPoly APoly(A)-Binding ProteinsProtein BindingRNADNA-Directed DNA PolymeraseExoribonucleasesExosome Multienzyme Ribonuclease ComplexNAB2 protein, S cerevisiaeNucleocytoplasmic Transport Proteinspab1 protein, S cerevisiaePAP2 protein, S cerevisiaePoly APoly(A)-Binding ProteinsRNARNA-Binding ProteinsRNA, MessengerRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22683267
PMCPMC3408791
OpenAlexW2052606860

What OpenQuestion holds

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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.