Evidence map›Paper›PMID 21847092›Full record

ArticleThe EMBO journal2011

An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer.

Pierre Barraud, Stephan Emmerth, Yukiko Shimada, Hans-Rudolf Hotz, Frédéric H-T Allain, Marc Bühler

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
10.7field-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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 48 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

6 authors at 2 institutions in 1 country.

Pierre BarraudInstitute of Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland.
Stephan Emmerth
Yukiko Shimada
Hans-Rudolf Hotz
Frédéric H-T Allain
Marc Bühler
Friedrich Miescher Institute · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here, we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast, disruption of zinc coordination renders Dcr1 mainly cytoplasmic and leads to remarkable changes in gene expression and loss of heterochromatin assembly. In summary, our results reveal novel insights into the mechanism of nuclear retention of Dcr1 and raise the possibility that this new class of dsRBDs might generally function in nucleocytoplasmic trafficking and not substrate binding. The C-terminal domain of Dcr1 constitutes a novel regulatory module that might represent a potential target for therapeutic intervention with fungal diseases.

Indexed as

Amino Acid MotifsAmino Acid SequenceCell NucleusChromatin Assembly and DisassemblyEndoribonucleasesMolecular Sequence DataProtein Structure, SecondaryRibonuclease IIIRNA-Binding ProteinsRNA, Double-StrandedSchizosaccharomycesSchizosaccharomyces pombe ProteinsZincDcr1 protein, S pombeEndoribonucleasesRibonuclease IIIRNA-Binding ProteinsRNA, Double-StrandedSchizosaccharomyces pombe ProteinsZinc

Identifiers

PMID21847092
PMCPMC3199388
OpenAlexW1578369217

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.