Evidence map›Paper›PMID 24145821›Full record

ArticleRNA (New York, N.Y.)2013

3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors.

Ivan Sabath, Aleksandra Skrajna, Xiao-Cui Yang, Michal Dadlez, William F Marzluff, Zbigniew Dominski

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  8. Review
  9. Review
  10. Replication-dependent histone biosynthesis is coupled to cell-cycle commitment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Superresolution light microscopy of theMolecular biology of the cell · 2021
    Article
  12. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Regulation of embryonic and adult neurogenesis by Ars2.Development (Cambridge, England) · 2020
    Article
  20. 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

6 authors at 2 institutions in 2 countries.

Ivan Sabath
Aleksandra Skrajna
Xiao-Cui Yang
Michal Dadlez
William F Marzluff
Zbigniew Dominski
University of North Carolina at Chapel Hill · USInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

HISTONE MRNA REGULATION IN DEVELOPMENTR01GM058921 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DURONIO, ROBERT J, MARZLUFF, WILLIAM F. · 1999 to 2025
$11.6M
NIGMS NIH HHS GM58921NIGMS NIH HHS R01 GM058921
6 · The paper itself

Abstract

3'-End cleavage of animal replication-dependent histone pre-mRNAs is controlled by the U7 snRNP. Lsm11, the largest component of the U7-specific Sm ring, interacts with FLASH, and in mammalian nuclear extracts these two proteins form a platform that recruits the CPSF73 endonuclease and other polyadenylation factors to the U7 snRNP. FLASH is limiting, and the majority of the U7 snRNP in mammalian extracts exists as a core particle consisting of the U7 snRNA and the Sm ring. Here, we purified the U7 snRNP from Drosophila nuclear extracts and characterized its composition by mass spectrometry. In contrast to the mammalian U7 snRNP, a significant fraction of the Drosophila U7 snRNP contains endogenous FLASH and at least six subunits of the polyadenylation machinery: symplekin, CPSF73, CPSF100, CPSF160, WDR33, and CstF64. The same composite U7 snRNP is recruited to histone pre-mRNA for 3'-end processing. We identified a motif in Drosophila FLASH that is essential for the recruitment of the polyadenylation complex to the U7 snRNP and analyzed the role of other factors, including SLBP and Ars2, in 3'-end processing of Drosophila histone pre-mRNAs. SLBP that binds the upstream stem-loop structure likely recruits a yet-unidentified essential component(s) to the processing machinery. In contrast, Ars2, a protein previously shown to interact with FLASH in mammalian cells, is dispensable for processing in Drosophila. Our studies also demonstrate that Drosophila symplekin and three factors involved in cleavage and polyadenylation-CPSF, CstF, and CF Im-are present in Drosophila nuclear extracts in a stable supercomplex.

Indexed as

RNA 3' End ProcessingAmino Acid SequenceAnimalsCarrier ProteinsCell LineCleavage And Polyadenylation Specificity FactorDrosophila melanogasterDrosophila ProteinsHistonesMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesNuclear ProteinsProtein Interaction MappingProtein SubunitsRibonucleoproteins, Small NuclearArs2 protein, DrosophilaCarrier ProteinsCleavage And Polyadenylation Specificity FactorDrosophila ProteinsFLASH protein, DrosophilaHistonesLsm11 protein, DrosophilamRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesNuclear ProteinsProtein SubunitsRibonucleoproteins, Small NuclearRibonucleoprotein, U7 Small NuclearRNA, MessengerRNA PrecursorsSym protein, Drosophila3′-end processingArs2CPSF73 endonucleaseDrosophila U7 snRNPFLASHhistone pre-mRNALsm11polyadenylation factorsSLBP

Identifiers

PMID24145821
PMCPMC3884669
OpenAlexW2104099845

What OpenQuestion holds

Textmetadata
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.