Evidence map›Paper›PMID 25104024›Full record

ArticleNucleic acids research2014

Regulation of pri-miRNA processing by the hnRNP-like protein AtGRP7 in Arabidopsis.

Tino Köster, Katja Meyer, Claus Weinholdt, Lisa M Smith, Martina Lummer, Corinna Speth, Ivo Grosse, Detlef Weigel, Dorothee Staiger

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

48 citing papers in PubMed, 108 citations in OpenAlex.

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  12. Du13 encodes a CPlant biotechnology journal · 2022
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  19. Improved Functional Expression of Cytochrome P450s inFrontiers in bioengineering and biotechnology · 2021
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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

9 authors at 5 institutions in 2 countries.

Tino KösterMolecular Cell Physiology, Bielefeld University.
Katja MeyerMolecular Cell Physiology, Bielefeld University.
Claus WeinholdtInstitute of Computer Science, Martin-Luther-University Halle-Wittenberg, Germany.
Lisa M SmithMax Planck Institute for Developmental Biology, Tuebingen, Germany Department of Animal & Plant Sciences, University of Sheffield, UK.
Martina LummerMolecular Cell Physiology, Bielefeld University.
Corinna SpethMax Planck Institute for Developmental Biology, Tuebingen, Germany Center for Plant Molecular Biology, University of Tuebingen Chemical Genomics Centre of the Max Planck Society, Dortmund, Germany.
Ivo GrosseInstitute of Computer Science, Martin-Luther-University Halle-Wittenberg, Germany German Centre for Integrative Biodiversity Research Halle-Jena-Leipzig, Germany.
Detlef WeigelMax Planck Institute for Developmental Biology, Tuebingen, Germany.
Dorothee StaigerMolecular Cell Physiology, Bielefeld University Institute for Genome Research & Systems Biology, CeBiTec, Bielefeld, Germany dorothee.staiger@uni-bielefeld.de.
Bielefeld University · DEMartin Luther University Halle-Wittenberg · DEChemical Genomics Centre · DEMax Planck Institute for Developmental Biology · DEUniversity of Sheffield · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hnRNP-like glycine-rich RNA-binding protein AtGRP7 regulates pre-mRNA splicing in Arabidopsis. Here we used small RNA-seq to show that AtGRP7 also affects the miRNA inventory. AtGRP7 overexpression caused a significant reduction in the level of 30 miRNAs and an increase for 14 miRNAs with a minimum log2 fold change of ± 0.5. Overaccumulation of several pri-miRNAs including pri-miR398b, pri-miR398c, pri-miR172b, pri-miR159a and pri-miR390 at the expense of the mature miRNAs suggested that AtGRP7 affects pri-miRNA processing. Indeed, RNA immunoprecipitation revealed that AtGRP7 interacts with these pri-miRNAs in vivo. Mutation of an arginine in the RNA recognition motif abrogated in vivo binding and the effect on miRNA and pri-miRNA levels, indicating that AtGRP7 inhibits processing of these pri-miRNAs by direct binding. In contrast, pri-miRNAs of selected miRNAs that were elevated or not changed in response to high AtGRP7 levels were not bound in vivo. Reduced accumulation of miR390, an initiator of trans-acting small interfering RNA (ta-siRNA) formation, also led to lower TAS3 ta-siRNA levels and increased mRNA expression of the target AUXIN RESPONSE FACTOR4. Furthermore, AtGRP7 affected splicing of pri-miR172b and pri-miR162a. Thus, AtGRP7 is an hnRNP-like protein with a role in processing of pri-miRNAs in addition to its role in pre-mRNA splicing.

Indexed as

Gene Expression Regulation, PlantRNA Processing, Post-TranscriptionalAlternative SplicingArabidopsisArabidopsis ProteinsMicroRNAsMolecular ChaperonesRNA-Binding ProteinsRNA, Small InterferingSuperoxide DismutaseArabidopsis ProteinsCSD2 protein, ArabidopsisGRP7 protein, ArabidopsisGRP8 protein, ArabidopsisMicroRNAsMIRN398 microRNA, ArabidopsisMolecular ChaperonesRNA-Binding ProteinsRNA, Small InterferingSuperoxide Dismutase

Identifiers

PMID25104024
PMCPMC4150807
OpenAlexW2106642163

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.