Evidence map›Paper›PMID 26101256›Full record

ArticleNucleic acids research2015

Induced folding in RNA recognition by Arabidopsis thaliana DCL1.

Irina P Suarez, Paula Burdisso, Matthieu P M H Benoit, Jèrôme Boisbouvier, Rodolfo M Rasia

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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

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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

5 authors at 3 institutions in 2 countries.

Irina P SuarezInstituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina.
Paula BurdissoInstituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina.
Matthieu P M H BenoitCEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France Université Joseph Fourier - Grenoble 1, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France.
Jèrôme BoisbouvierCEA, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France CNRS, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France Université Joseph Fourier - Grenoble 1, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France.
Rodolfo M RasiaInstituto de Biología Molecular y Celular de Rosario. 27 de Febrero 210 bis, predio CCT, 2000 Rosario, Argentina Área Biofísica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Suipacha 531, 2000 Rosario, Argentina rasia@ibr-conicet.gov.ar.
CEA Grenoble · FRInstituto de Biología Molecular y Celular de Rosario · ARNational University of Rosario · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DCL1 is the ribonuclease that carries out miRNA biogenesis in plants. The enzyme has two tandem double stranded RNA binding domains (dsRBDs) in its C-terminus. Here we show that the first of these domains binds precursor RNA fragments when isolated and cooperates with the second domain in the recognition of substrate RNA. Remarkably, despite showing RNA binding activity, this domain is intrinsically disordered. We found that it acquires a folded conformation when bound to its substrate, being the first report of a complete dsRBD folding upon binding. The free unfolded form shows tendency to adopt folded conformations, and goes through an unfolded bound state prior to the folding event. The significance of these results is discussed by comparison with the behavior of other dsRBDs.

Indexed as

Arabidopsis ProteinsCell Cycle ProteinsIntrinsically Disordered ProteinsModels, MolecularProtein BindingProtein StabilityProtein Structure, TertiaryRibonuclease IIIRNARNA-Binding ProteinsRNA FoldingArabidopsis ProteinsCell Cycle ProteinsDCL1 protein, ArabidopsisIntrinsically Disordered ProteinsRibonuclease IIIRNARNA-Binding Proteins

Identifiers

PMID26101256
PMCPMC4513881
OpenAlexW1874976195

What OpenQuestion holds

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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.