Evidence map›Paper›PMID 24255165›Full record

ArticleRNA (New York, N.Y.)2014

The C-terminal extension of Lsm4 interacts directly with the 3' end of the histone mRNP and is required for efficient histone mRNA degradation.

Shawn M Lyons, Adele S Ricciardi, Andrew Y Guo, Christian Kambach, William F Marzluff

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Yeast Lsm Pro-Apoptotic Mutants Show Defects in Autophagy.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Role of oligouridylation in normal metabolism and regulated degradation of mammalian histone mRNAs.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  15. Review
  16. Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Uridylation and adenylation of RNAs.Science China. Life sciences · 2015
    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

5 authors at 2 institutions in 2 countries.

Shawn M Lyons
Adele S Ricciardi
Andrew Y Guo
Christian Kambach
William F Marzluff
University of North Carolina at Chapel Hill · USUniversity of Bayreuth · DE

Funding

CONTROL OF HISTONE MRNA SYNTHESISR01GM029832 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOMINSKI, ZBIGNIEW, MARZLUFF, WILLIAM F. · 1985 to 2022
$9.0M
NIGMS NIH HHS GM29832NIGMS NIH HHS R01 GM029832
6 · The paper itself

Abstract

Metazoan replication-dependent histone mRNAs are the only known eukaryotic mRNAs that lack a poly(A) tail, ending instead in a conserved stem-loop sequence, which is bound to the stem-loop binding protein (SLBP) on the histone mRNP. Histone mRNAs are rapidly degraded when DNA synthesis is inhibited in S phase in mammalian cells. Rapid degradation of histone mRNAs is initiated by oligouridylation of the 3' end of histone mRNAs and requires the cytoplasmic Lsm1-7 complex, which can bind to the oligo(U) tail. An exonuclease, 3'hExo, forms a ternary complex with SLBP and the stem-loop and is required for the initiation of histone mRNA degradation. The Lsm1-7 complex is also involved in degradation of polyadenylated mRNAs. It binds to the oligo(A) tail remaining after deadenylation, inhibiting translation and recruiting the enzymes required for decapping. Whether the Lsm1-7 complex interacts directly with other components of the mRNP is not known. We report here that the C-terminal extension of Lsm4 interacts directly with the histone mRNP, contacting both SLBP and 3'hExo. Mutants in the C-terminal tail of Lsm4 that prevent SLBP and 3'hExo binding reduce the rate of histone mRNA degradation when DNA synthesis is inhibited.

Indexed as

3' Flanking RegionRNA StabilityAmino Acid SequenceBase SequenceHeLa CellsHistonesHumansMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsNuclear ProteinsProtein BindingProtein Interaction Domains and MotifsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA, MessengerHistonesLSM4 protein, humanmessenger ribonucleoproteinmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA, MessengerSLBP protein, humanERI1histone mRNALsm proteinsmRNA degradationSLBP

Identifiers

PMID24255165
PMCPMC3866647
OpenAlexW2031969229

What OpenQuestion holds

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LicenceCC BY-NC
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.