Evidence map›Paper›PMID 11514438›Full record

ArticleGenetics2001

The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation.

W He, R Parker

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Yeast Lsm Pro-Apoptotic Mutants Show Defects in Autophagy.International journal of molecular sciences · 2023
    Article
  6. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  7. Variants inHGG advances · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Pat1 activates late steps in mRNA decay by multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

1 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 2 institutions in 1 country.

W HeDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.
R Parker
Howard Hughes Medical Institute · USUniversity of Arizona · US

Funding

Stress Granules in Yeast and MammalsR01GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 1991 to 2021
$3.3M
mRNA Decapping in YeastR37GM045443 · NIGMS · UNIVERSITY OF COLORADO · PI PARKER, ROY · 2004 to 2013
$3.1M
NIGMS NIH HHS GM-45443
6 · The paper itself

Abstract

A key aspect of understanding eukaryotic gene regulation will be the identification and analysis of proteins that bind mRNAs and control their function. Recently, a complex of seven Lsm proteins and the Pat1p have been shown to interact with yeast mRNAs and promote mRNA decapping. In this study we present several observations to indicate that the LsmI/Pat1 complex has a second distinct function in protecting the 3'-UTR of mRNAs from trimming. First, mutations in the LSM1 to LSM7, as well as PAT1, genes led to the accumulation of MFA2pG and PGK1pG transcripts that had been shortened by 10-20 nucleotides at their 3' ends (referred to as trimming). Second, the trimming of these mRNAs was more severe at the high temperature, correlating with the inability of these mutant strains to grow at high temperature. In contrast, trimming did not occur in a dcp1 Delta strain, wherein the decapping enzyme is lacking. This indicates that trimming is not simply a consequence of the inhibition of mRNA decapping. Third, the temperature-sensitive growth of lsm and pat1 mutants was suppressed by mutations in the exosome or the functionally related Ski proteins, which are required for efficient 3' to 5' mRNA degradation of mRNA. Moreover, in lsm ski double mutants, higher levels of the trimmed mRNAs accumulated, indicating that exosome function is not required for mRNA trimming but that the exosome does degrade the trimmed mRNAs. These results raise the possibility that the temperature-sensitive growth of the lsm1-7 and pat1 mutants is at least partially due to mRNA trimming, which either inactivates the function of the mRNAs or makes them available for premature 3' to 5' degradation by the exosome.

Indexed as

RNA-Binding ProteinsSaccharomyces cerevisiae Proteins3' Untranslated RegionsBlotting, NorthernCell DivisionCytoplasmDNA-Binding ProteinsFungal ProteinsFungiModels, GeneticMutationPhenotypePlasmidsProtein BindingProto-Oncogene ProteinsRNA Cap-Binding Proteins3' Untranslated RegionsDNA-Binding ProteinsFungal ProteinsLSM1 protein, S cerevisiaePAT1 protein, S cerevisiaeProto-Oncogene ProteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA CapsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID11514438
PMCPMC1461746
OpenAlexW2117764830

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.