Evidence map›Paper›PMID 23071092›Full record

ArticleMolecular and cellular biology2013

A complex containing the CPSF73 endonuclease and other polyadenylation factors associates with U7 snRNP and is recruited to histone pre-mRNA for 3'-end processing.

Xiao-Cui Yang, Ivan Sabath, Jan Dębski, Magdalena Kaus-Drobek, Michał Dadlez, William F Marzluff, Zbigniew Dominski

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed, 76 citations in OpenAlex.

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  18. 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
  19. Article
  20. Superresolution light microscopy of theMolecular biology of the cell · 2021
    Article

2 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Xiao-Cui YangDepartment of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Ivan Sabath
Jan Dębski
Magdalena Kaus-Drobek
Michał Dadlez
William F Marzluff
Zbigniew Dominski
University of North Carolina at Chapel Hill · USInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLUniversity of Warsaw · PL

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

Animal replication-dependent histone pre-mRNAs are processed at the 3' end by endonucleolytic cleavage that is not followed by polyadenylation. The cleavage reaction is catalyzed by CPSF73 and depends on the U7 snRNP and its integral component, Lsm11. A critical role is also played by the 220-kDa protein FLASH, which interacts with Lsm11. Here we demonstrate that the N-terminal regions of these two proteins form a platform that tightly interacts with a unique combination of polyadenylation factors: symplekin, CstF64, and all CPSF subunits, including the endonuclease CPSF73. The interaction is inhibited by alterations in each component of the FLASH/Lsm11 complex, including point mutations in FLASH that are detrimental for processing. The same polyadenylation factors are associated with the endogenous U7 snRNP and are recruited in a U7-dependent manner to histone pre-mRNA. Collectively, our studies identify the molecular mechanism that recruits the CPSF73 endonuclease to histone pre-mRNAs, reveal an unexpected complexity of the U7 snRNP, and suggest that in animal cells polyadenylation factors assemble into two alternative complexes-one specifically crafted to generate polyadenylated mRNAs and the other to generate nonpolyadenylated histone mRNAs that end with the stem-loop.

Indexed as

RNA 3' End ProcessingAmino Acid MotifsAnimalsApoptosis Regulatory ProteinsBase SequenceCalcium-Binding ProteinsCleavage And Polyadenylation Specificity FactorCleavage Stimulation FactorHeLa CellsHistonesHumansMiceMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsMutationNuclear ProteinsApoptosis Regulatory ProteinsCalcium-Binding ProteinsCASP8AP2 protein, humanCleavage And Polyadenylation Specificity FactorCleavage Stimulation FactorCSTF2T protein, humanHistonesLSM11 protein, humanmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRecombinant ProteinsRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA PrecursorsSYMPK protein, human

Identifiers

PMID23071092
PMCPMC3536302
OpenAlexW2151039523

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.