Evidence map›Paper›PMID 27780203›Full record

ArticlePLoS biology2016

snRNA 3' End Processing by a CPSF73-Containing Complex Essential for Development in Arabidopsis.

Yunfeng Liu, Shengjun Li, Yuan Chen, Athen N Kimberlin, Edgar B Cahoon, Bin Yu

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2016. 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
0.7field-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, 28 citations in OpenAlex.

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  9. An antisense intragenic lncRNA SEAIRa mediates transcriptional and epigenetic repression ofProceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 2 institutions in 1 country.

Yunfeng LiuCenter for Plant Science Innovation and School of Biological Sciences, University of Nebraska, Lincoln, Nebraska, United States of America.ORCID http://orcid.org/0000-0002-4166-9056
Shengjun LiCenter for Plant Science Innovation and School of Biological Sciences, University of Nebraska, Lincoln, Nebraska, United States of America.
Yuan ChenPlant Gene Expression Center, US Department of Agriculture-Agricultural Research Service, University of California-Berkeley, Albany, California, United States of America.
Athen N KimberlinCenter for Plant Science Innovation and Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, United States of America.
Edgar B CahoonCenter for Plant Science Innovation and Department of Biochemistry, University of Nebraska, Lincoln, Nebraska, United States of America.
Bin YuCenter for Plant Science Innovation and School of Biological Sciences, University of Nebraska, Lincoln, Nebraska, United States of America.
University of Nebraska–Lincoln · USPlant Gene Expression Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uridine-rich small nuclear RNAs (snRNAs) are the basal components of the spliceosome and play essential roles in splicing. The biogenesis of the majority of snRNAs involves 3' end endonucleolytic cleavage of the nascent transcript from the elongating DNA-dependent RNA ploymerase II. However, the protein factors responsible for this process remain elusive in plants. Here, we show that DEFECTIVE in snRNA PROCESSING 1 (DSP1) is an essential protein for snRNA 3' end maturation in Arabidopsis. A hypomorphic dsp1-1 mutation causes pleiotropic developmental defects, impairs the 3' end processing of snRNAs, increases the levels of snRNA primary transcripts (pre-snRNAs), and alters the occupancy of Pol II at snRNA loci. In addition, DSP1 binds snRNA loci and interacts with Pol-II in a DNA/RNA-dependent manner. We further show that DSP1 forms a conserved complex, which contains at least four additional proteins, to catalyze snRNA 3' end maturation in Arabidopsis. The catalytic component of this complex is likely the cleavage and polyadenylation specificity factor 73 kDa-I (CSPF73-I), which is the nuclease cleaving the pre-mRNA 3' end. However, the DSP1 complex does not affect pre-mRNA 3' end cleavage, suggesting that plants may use different CPSF73-I-containing complexes to process snRNAs and pre-mRNAs. This study identifies a complex responsible for the snRNA 3' end maturation in plants and uncovers a previously unknown function of CPSF73 in snRNA maturation.

Indexed as

RNA Processing, Post-TranscriptionalArabidopsisArabidopsis ProteinsCleavage And Polyadenylation Specificity FactorGenes, PlantMutationPollenRNA, Small NuclearArabidopsis ProteinsCleavage And Polyadenylation Specificity FactorRNA, Small Nuclear

Identifiers

PMID27780203
PMCPMC5079582
OpenAlexW2534431882

What OpenQuestion holds

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Registered trials

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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.