Evidence map›Paper›PMID 30397106›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018

Role of oligouridylation in normal metabolism and regulated degradation of mammalian histone mRNAs.

Stacie A Meaux, Christopher E Holmquist, William F Marzluff

Open access · bronzeAbstract read
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Measuring the tail: Methods for poly(A) tail profiling.Wiley interdisciplinary reviews. RNA · 2023
    Review
  11. Article
  12. Review
  13. Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  14. The role of 3' end uridylation in RNA metabolism and cellular physiology.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  15. 5' and 3' modifications controlling RNA degradation: from safeguards to executioners.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
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

3 authors at 1 institution in 1 country.

Stacie A MeauxDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.ORCID 0000-0001-9055-5664
Christopher E HolmquistDepartment of Medicinal Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA.
William F MarzluffDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA marzluff@med.unc.edu.ORCID 0000-0003-3635-4073
University of North Carolina at Chapel Hill · US

Funding

CONTROL OF HISTONE MRNA SYNTHESISR01GM029832 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOMINSKI, ZBIGNIEW, MARZLUFF, WILLIAM F. · 1985 to 2022
$9.0M
A Novel Factor Involved in Translation of Histone mRNA and Subsets of PolyA mRNAF32GM080007 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LERNER, RACHEL S. · 2008 to 2009
$65k
NIGMS NIH HHS F32 GM080007NIGMS NIH HHS R01 GM029832
6 · The paper itself

Abstract

Metazoan replication-dependent histone mRNAs are the only known cellular mRNAs that are not polyadenylated. Histone mRNAs are present in large amounts only in S-phase cells, and their levels are coordinately regulated with the rate of DNA replication. In mammals, the stemloop at the 3' end of histone mRNA is bound to stemloop binding protein, a protein required for both synthesis and degradation of histone mRNA, and an exonuclease, 3'hExo (ERI1). Histone mRNAs are rapidly degraded when DNA synthesis is inhibited in S-phase cells and at the end of S-phase. Upf1 is also required for rapid degradation of histone mRNA as is the S-phase checkpoint. We report that Smg1 is required for histone mRNA degradation when DNA replication is inhibited, suggesting it is the PI-like kinase that activates Upf1 for histone mRNA degradation. We also show that some mutant Upf1 proteins are recruited to histone mRNAs when DNA replication is inhibited and act as dominant negative factors in histone mRNA degradation. We report that the pathway of rapid histone mRNA degradation when DNA replication is inhibited in S-phase cells that are activating the S-phase checkpoint is similar to the pathway of rapid degradation of histone mRNA at the end of S-phase.This article is part of the theme issue '5' and 3' modifications controlling RNA degradation'.

Indexed as

DNA ReplicationRNA StabilityHeLa CellsHistonesHumansPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesRNA, MessengerUridineHistonesPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesRNA, MessengerSMG1 protein, humanUridinecell cyclehistone mRNARNA degradationuridylation

Identifiers

PMID30397106
PMCPMC6232589
OpenAlexW2900372684

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.