Evidence map›Paper›PMID 10611239›Full record

ArticleMolecular and cellular biology2000

A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p.

K T Burkard, J S Butler

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
4.8field-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

112 citing papers in PubMed, 210 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Polyadenylated versions of small non-coding RNAs inMicrobial cell (Graz, Austria) · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The RNA Exosome and Human Disease.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  14. RNA Exosomes and Their Cofactors.Methods in molecular biology (Clifton, N.J.) · 2020
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Stress-induced nuclear depletion ofThe Journal of biological chemistry · 2018
    Article
  20. Review

52 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

K T BurkardDepartment of Microbiology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14618, USA.
J S Butler
University of Rochester · US

Funding

NUCLEAR PATHWAY FOR MESSENGER RNA DEGRADATION IN YEASTR01GM059898 · NIGMS · UNIVERSITY OF ROCHESTER · PI BUTLER, JAMES SCOTT · 1999 to 2002
$831k
NIGMS NIH HHS GM 59898NIGMS NIH HHS R01 GM059898
6 · The paper itself

Abstract

Inactivation of poly(A) polymerase (encoded by PAP1) in Saccharomyces cerevisiae cells carrying the temperature-sensitive, lethal pap1-1 mutation results in reduced levels of poly(A)(+) mRNAs. Genetic selection for suppressors of pap1-1 yielded two recessive, cold-sensitive alleles of the gene RRP6. These suppressors, rrp6-1 and rrp6-2, as well as a deletion of RRP6, allow growth of pap1-1 strains at high temperature and partially restore the levels of poly(A)(+) mRNA in a manner distinct from the cytoplasmic mRNA turnover pathway and without slowing a rate-limiting step in mRNA decay. Subcellular localization of an Rrp6p-green fluorescent protein fusion shows that the enzyme residues in the nucleus. Phylogenetic analysis and the nature of the rrp6-1 mutation suggest the existence of a highly conserved 3'-5' exonuclease core domain within Rrp6p. As predicted, recombinant Rrp6p catalyzes the hydrolysis of a synthetic radiolabeled RNA in a manner consistent with a 3'-5' exonucleolytic mechanism. Genetic and biochemical experiments indicate that Rrp6p interacts with poly(A) polymerase and with Npl3p, a poly(A)(+) mRNA binding protein implicated in pre-mRNA processing and mRNA nuclear export. These findings suggest that Rrp6p may interact with the mRNA polyadenylation system and thereby play a role in a nuclear pathway for the degradation of aberrantly processed precursor mRNAs.

Indexed as

RNA-Binding ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceCatalytic DomainCell NucleusExoribonucleasesExosome Multienzyme Ribonuclease ComplexFungal ProteinsGenes, FungalHalf-LifeMolecular Sequence DataMutationNuclear ProteinsPancreatitis-Associated ProteinsPolynucleotide AdenylyltransferaseProtein BindingExoribonucleasesExosome Multienzyme Ribonuclease ComplexFungal ProteinsNPL3 protein, S cerevisiaeNuclear ProteinsPancreatitis-Associated ProteinsPolynucleotide AdenylyltransferaseRecombinant Fusion ProteinsREG3A protein, humanRNA-Binding ProteinsRNA, FungalRNA, Heterogeneous NuclearRNA, MessengerRRP6 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID10611239
PMCPMC85144
OpenAlexW2040010148

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.