Evidence map›Paper›PMID 26769856›Full record

ArticleRNA (New York, N.Y.)2016

Structural and functional insights into the fly microRNA biogenesis factor Loquacious.

Leonhard Jakob, Thomas Treiber, Nora Treiber, Alexander Gust, Kevin Kramm, Kerrin Hansen, Mathias Stotz, Ludwig Wankerl, Franz Herzog, Stefan Hannus and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 12 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

12 authors at 3 institutions in 1 country.

Leonhard JakobBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Thomas TreiberBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Nora TreiberBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Alexander GustDepartment of Microbiology and Archaea Centre, Laboratory of Single-Molecule Biochemistry, University of Regensburg, 93053 Regensburg, Germany.
Kevin KrammDepartment of Microbiology and Archaea Centre, Laboratory of Single-Molecule Biochemistry, University of Regensburg, 93053 Regensburg, Germany.
Kerrin HansenIntana Bioscience GmbH, 82152 Planegg, Martinsried, Germany.
Mathias StotzBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Ludwig WankerlBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
Franz HerzogGene Center and Department of Biochemistry, Ludwig-Maximilians-University, 81377 München, Germany.
Stefan HannusIntana Bioscience GmbH, 82152 Planegg, Martinsried, Germany.
Dina GrohmannDepartment of Microbiology and Archaea Centre, Laboratory of Single-Molecule Biochemistry, University of Regensburg, 93053 Regensburg, Germany.
Gunter MeisterBiochemistry Center Regensburg (BZR), Laboratory for RNA Biology, University of Regensburg, 93053 Regensburg, Germany.
University of Regensburg · DEMax Planck Institute of Biochemistry · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the microRNA (miRNA) pathway, Dicer processes precursors to mature miRNAs. For efficient processing, double-stranded RNA-binding proteins support Dicer proteins. In flies, Loquacious (Loqs) interacts with Dicer1 (dmDcr1) to facilitate miRNA processing. Here, we have solved the structure of the third double-stranded RNA-binding domain (dsRBD) of Loqs and define specific structural elements that interact with dmDcr1. In addition, we show that the linker preceding dsRBD3 contributes significantly to dmDcr1 binding. Furthermore, our structural work demonstrates that the third dsRBD of Loqs forms homodimers. Mutations in the dimerization interface abrogate dmDcr1 interaction. Loqs, however, binds to dmDcr1 as a monomer using the identified dimerization surface, which suggests that Loqs might form dimers under conditions where dmDcr1 is absent or not accessible. Since critical sequence elements are conserved, we suggest that dimerization might be a general feature of dsRBD proteins in gene silencing.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayDimerizationDrosophila melanogasterDrosophila ProteinsGene SilencingHumansMicroRNAsMolecular Sequence DataMutationProtein BindingProtein ConformationRNA-Binding ProteinsSequence Homology, Amino AcidSpectrometry, FluorescenceDrosophila ProteinsLoqs protein, DrosophilaMicroRNAsRNA-Binding ProteinsDicerDrosophiladsRBDfluorescence spectroscopygene silencingLoquaciousmicroRNA

Identifiers

PMID26769856
PMCPMC4748816
OpenAlexW2236931196

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.