Evidence map›Paper›PMID 30139799›Full record

ArticleRNA (New York, N.Y.)2018

Reconstitution of mammalian cleavage factor II involved in 3' processing of mRNA precursors.

Peter Schäfer, Christian Tüting, Lars Schönemann, Uwe Kühn, Thomas Treiber, Nora Treiber, Christian Ihling, Anne Graber, Walter Keller, Gunter Meister and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2018. 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
2.0field-weighted citation impact, top 12% 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, 55 citations in OpenAlex.

  1. Review
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  10. Premature transcription termination complex proteins PCF11 and WDR82 silence HIV-1 expression in latently infected cells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  15. Plant terminators: the unsung heroes of gene expression.Journal of experimental botany · 2023
    Review
  16. Article
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  18. Molecular Insights into mRNA Polyadenylation and Deadenylation.International journal of molecular sciences · 2022
    Review
  19. Review
  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

12 authors at 3 institutions in 2 countries.

Peter SchäferInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Christian TütingInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Lars SchönemannInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Uwe KühnInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Thomas TreiberBiochemistry Center Regensburg, Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Nora TreiberBiochemistry Center Regensburg, Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Christian IhlingInstitute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Anne GraberInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Walter KellerBiozentrum, University of Basel, CH-4056 Basel, Switzerland.
Gunter MeisterBiochemistry Center Regensburg, Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Andrea SinzInstitute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
Elmar WahleInstitute of Biochemistry and Biotechnology, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.ORCID 0000-0003-2504-0677
Martin Luther University Halle-Wittenberg · DEUniversity of Regensburg · DEUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cleavage factor II (CF II) is a poorly characterized component of the multiprotein complex catalyzing 3' cleavage and polyadenylation of mammalian mRNA precursors. We have reconstituted CF II as a heterodimer of hPcf11 and hClp1. The heterodimer is active in partially reconstituted cleavage reactions, whereas hClp1 by itself is not. Pcf11 moderately stimulates the RNA 5' kinase activity of hClp1; the kinase activity is dispensable for RNA cleavage. CF II binds RNA with nanomolar affinity. Binding is mediated mostly by the two zinc fingers in the C-terminal region of hPcf11. RNA is bound without pronounced sequence-specificity, but extended G-rich sequences appear to be preferred. We discuss the possibility that CF II contributes to the recognition of cleavage/polyadenylation substrates through interaction with G-rich far-downstream sequence elements.

Indexed as

Binding SitesmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesNuclear ProteinsPhosphotransferasesPolyadenylationProtein BindingProtein MultimerizationRNA PrecursorsSequence Homology, Amino AcidTranscription FactorsCLP1 protein, humanmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesNuclear ProteinsPcf11 protein, humanPhosphotransferasesRNA PrecursorsTranscription Factors3′ end formationClp1mRNA processingPcf11polyadenylation

Identifiers

PMID30139799
PMCPMC6239180
OpenAlexW2950403225

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.