Evidence map›Paper›PMID 18719247›Full record

ArticleRNA (New York, N.Y.)2008

lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo.

Ashis Chowdhury, Sundaresan Tharun

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  9. Article
  10. Review
  11. Deadenylation and P-bodies.Advances in experimental medicine and biology · 2013
    Review
  12. Article
  13. Article
  14. Article
  15. Article
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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

2 authors at 1 institution in 1 country.

Ashis ChowdhuryDepartment of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799, USA.
Sundaresan Tharun
Uniformed Services University of the Health Sciences · US

Funding

Role of the Yeast Lsm Proteins in mRNA DecayR01GM072718 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI SUNDARESAN, THARUN · 2006 to 2010
$1.2M
NIGMS NIH HHS GM072718NIGMS NIH HHS R01 GM072718
6 · The paper itself

Abstract

The poly(A) tail is a crucial determinant in the control of both mRNA translation and decay. Poly(A) tail length dictates the triggering of the degradation of the message body in the major 5' to 3' and 3' to 5' mRNA decay pathways of eukaryotes. In the 5' to 3' pathway oligoadenylated but not polyadenylated mRNAs are selectively decapped in vivo, allowing their subsequent degradation by 5' to 3' exonucleolysis. The conserved Lsm1p-7p-Pat1p complex is required for normal rates of decapping in vivo, and the purified complex exhibits strong binding preference for oligoadenylated RNAs over polyadenylated or unadenylated RNAs in vitro. In the present study, we show that two lsm1 mutants produce mutant complexes that fail to exhibit such higher affinity for oligoadenylated RNA in vitro. Interestingly, these mutant complexes are normal with regard to their integrity and retain the characteristic RNA binding properties of the wild-type complex, namely, binding near the 3'-end of the RNA, having higher affinity for unadenylated RNAs that carry U-tracts near the 3'-end over those that do not and exhibiting similar affinities for unadenylated and polyadenylated RNAs. Yet, these lsm1 mutants exhibit a strong mRNA decay defect in vivo. These results underscore the importance of Lsm1p-7p-Pat1p complex-mRNA interaction for mRNA decay in vivo and imply that the oligo(A) tail mediated enhancement of such interaction is crucial in that process.

Indexed as

MutationPolyadenylationDNA-Binding ProteinsRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsLSM1 protein, S cerevisiaePAT1 protein, S cerevisiaeRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID18719247
PMCPMC2553750
OpenAlexW2139340906

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.