Evidence map›Paper›PMID 30247719›Full record

ArticleNucleic acids research2018

The APT complex is involved in non-coding RNA transcription and is distinct from CPF.

Michael Lidschreiber, Ashley D Easter, Sofia Battaglia, Juan B Rodríguez-Molina, Ana Casañal, Manuel Carminati, Carlo Baejen, Pawel Grzechnik, Kerstin C Maier, Patrick Cramer and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

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  11. 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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  17. Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021
    Review
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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

11 authors at 4 institutions in 3 countries.

Michael LidschreiberDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Ashley D EasterMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Sofia BattagliaDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Juan B Rodríguez-MolinaMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Ana CasañalMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Manuel CarminatiMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Carlo BaejenDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Pawel GrzechnikSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
Kerstin C MaierDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Patrick CramerDepartment of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Lori A PassmoreMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
MRC Laboratory of Molecular Biology · GBMax Planck Institute for Biophysical Chemistry · DEScience for Life Laboratory · SEUniversity of Birmingham · GB

Funding

European Research Council 261151European Research Council 693023Medical Research Council MC_U105192715Wellcome Trust 200473/Z/16/Z
6 · The paper itself

Abstract

The 3'-ends of eukaryotic pre-mRNAs are processed in the nucleus by a large multiprotein complex, the cleavage and polyadenylation factor (CPF). CPF cleaves RNA, adds a poly(A) tail and signals transcription termination. CPF harbors four enzymatic activities essential for these processes, but how these are coordinated remains poorly understood. Several subunits of CPF, including two protein phosphatases, are also found in the related 'associated with Pta1' (APT) complex, but the relationship between CPF and APT is unclear. Here, we show that the APT complex is physically distinct from CPF. The 21 kDa Syc1 protein is associated only with APT, and not with CPF, and is therefore the defining subunit of APT. Using ChIP-seq, PAR-CLIP and RNA-seq, we show that Syc1/APT has distinct, but possibly overlapping, functions from those of CPF. Syc1/APT plays a more important role in sn/snoRNA production whereas CPF processes the 3'-ends of protein-coding pre-mRNAs. These results define distinct protein machineries for synthesis of mature eukaryotic protein-coding and non-coding RNAs.

Indexed as

Transcription, GeneticChromatin ImmunoprecipitationmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesProtein SubunitsRNA, Small NucleolarRNA, UntranslatedSaccharomyces cerevisiae ProteinsmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesProtein SubunitsRNA, Small NucleolarRNA, UntranslatedSaccharomyces cerevisiae ProteinsSYC1 protein, S cerevisiae

Identifiers

PMID30247719
PMCPMC6265451
OpenAlexW2890630382

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.