Evidence map›Paper›PMID 25680966›Full record

ArticleNucleic acids research2015

Functional mapping of the plant small RNA methyltransferase: HEN1 physically interacts with HYL1 and DICER-LIKE 1 proteins.

Simona Baranauskė, Milda Mickutė, Alexandra Plotnikova, Andreas Finke, Česlovas Venclovas, Saulius Klimašauskas, Giedrius Vilkaitis

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
12.9field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 84 citations in OpenAlex.

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  12. RNA-Based Control of Fungal Pathogens in Plants.International journal of molecular sciences · 2023
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  19. microRNA production inFrontiers in plant science · 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

7 authors at 2 institutions in 2 countries.

Simona BaranauskėDepartment of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania.
Milda MickutėDepartment of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania.
Alexandra PlotnikovaDepartment of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania.
Andreas FinkeDepartment of Plant Breeding and Genetics, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.
Česlovas VenclovasDepartment of Bioinformatics, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania.
Saulius KlimašauskasDepartment of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania.
Giedrius VilkaitisDepartment of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-02241, Lithuania giedrius@ibt.lt.
Vilnius University · LTMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylation of 3'-terminal nucleotides of miRNA/miRNA* is part of miRNAs biogenesis in plants but is not found in animals. In Arabidopsis thaliana this reaction is carried out by a multidomain AdoMet-dependent 2'-O-methyltransferase HEN1. Using deletion and structure-guided mutational analysis, we show that the double-stranded RNA-binding domains R(1) and R(2) of HEN1 make significant but uneven contributions to substrate RNA binding, and map residues in each domain responsible for this function. Using GST pull-down assays and yeast two-hybrid analysis we demonstrate direct HEN1 interactions, mediated by its FK506-binding protein-like domain and R(2) domain, with the microRNA biogenesis protein HYL1. Furthermore, we find that HEN1 forms a complex with DICER-LIKE 1 (DCL1) ribonuclease, another key protein involved in miRNA biogenesis machinery. In contrast, no direct interaction is detectable between HEN1 and SERRATE. On the basis of these findings, we propose a mechanism of plant miRNA maturation which involves binding of the HEN1 methyltransferase to the DCL1•HYL1•miRNA complex excluding the SERRATE protein.

Indexed as

Amino Acid SequenceArabidopsis ProteinsCell Cycle ProteinsElectrophoretic Mobility Shift AssayMethylationMethyltransferasesMicroRNAsModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein Interaction MappingProtein Structure, TertiaryRibonuclease IIIRNA-Binding ProteinsArabidopsis ProteinsCell Cycle ProteinsDCL1 protein, ArabidopsisHEN1 protein, ArabidopsisHYL1 protein, ArabidopsisMethyltransferasesMicroRNAsRibonuclease IIIRNA 2'-O-methyltransferaseRNA-Binding ProteinsRNA, Plant

Identifiers

PMID25680966
PMCPMC4357707
OpenAlexW2171296576

What OpenQuestion holds

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LicenceCC BY-NC
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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.