Evidence map›Paper›PMID 17964263›Full record

ArticleMolecular cell2007

U2 snRNP binds intronless histone pre-mRNAs to facilitate U7-snRNP-dependent 3' end formation.

Kyle Friend, Alexander F Lovejoy, Joan A Steitz

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. The SF3b complex: splicing and beyond.Cellular and molecular life sciences : CMLS · 2020
    Review
  9. Article
  10. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
  11. Article
  12. A U2-snRNP-independent role of SF3b in promoting mRNA export.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Review
  15. Cajal body function in genome organization and transcriptome diversity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kyle FriendHoward Hughes Medical Institute, Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.
Alexander F Lovejoy
Joan A Steitz
Howard Hughes Medical Institute · US

Funding

Vertebrate Non-Coding RNPs: Integrating function, biogenesis and survivalR01GM026154 · NIGMS · YALE UNIVERSITY · PI STEITZ, JOAN A. · 1985 to 2014
$4.0M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM026154
6 · The paper itself

Abstract

In metazoa, pre-mRNA 3' end formation occurs via two pathways: cleavage/polyadenylation for the majority of RNA polymerase II transcripts and U7-snRNP-dependent cleavage for replication-dependent histone pre-mRNAs. An RNA element derived from a replication-dependent histone gene affects multiple steps of pre-mRNA processing. Here, we demonstrate that a portion of this RNA element, present in the majority of histone mRNAs, stimulates U7-snRNP-dependent cleavage. Surprisingly, this element binds U2 snRNP, although it is derived from an intronless mRNA. Specifically, SF3b, a U2 and U12-snRNP component, contacts the RNA element both in vitro and in vivo in conjunction with hPrp43, a DEAH-box helicase. Tethering either U2 or U12 snRNP to histone pre-mRNA substrates stimulates U7-snRNP-dependent cleavage in vitro and in vivo. Finally, we show that U2 snRNP associates with histone pre-mRNAs in vivo. We conclude that U2 snRNP plays a nonsplicing role in histone mRNA maturation.

Indexed as

RNA 3' End ProcessingAnimalsBase SequenceCell NucleusDEAD-box RNA HelicasesHeLa CellsHistonesHumansIntronsMiceModels, MolecularOocytesProtein ConformationRibonucleoproteins, Small NuclearRibonucleoprotein, U2 Small NuclearRibonucleoprotein, U7 Small NuclearDEAD-box RNA HelicasesHistonesRibonucleoproteins, Small NuclearRibonucleoprotein, U2 Small NuclearRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA PrecursorsU11-U12 small nuclear ribonucleoprotein

Identifiers

PMID17964263
PMCPMC2149891
OpenAlexW1971141018

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.