Evidence map›Paper›PMID 25778731›Full record

ArticleRNA (New York, N.Y.)2015

Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists.

Kuan-Ming Chen, Edgar Campbell, Radha Raman Pandey, Zhaolin Yang, Andrew A McCarthy, Ramesh S Pillai

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
6.7field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 30 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 1 institution in 1 country.

Kuan-Ming ChenEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Edgar CampbellEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Radha Raman PandeyEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Zhaolin YangEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Andrew A McCarthyEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Ramesh S PillaiEuropean Molecular Biology Laboratory, Grenoble Outstation, 38042 Grenoble Cedex 9, France Unit for Virus Host-Cell Interactions, University Grenoble Alpes-EMBL-CNRS, 38042 Grenoble Cedex 9, France.
Centre National de la Recherche Scientifique · FR

Funding

Genetic Control of Retrotransposon Mobilization in the Mouse GermlineR01HD069592 · NICHD · UNIVERSITY OF PENNSYLVANIA · PI WANG, PEIJING JEREMY · 2012 to 2023
$3.1M
NICHD NIH HHS 1R01HD069592-01A1NICHD NIH HHS R01 HD069592
6 · The paper itself

Abstract

Piwi-interacting RNAs (piRNAs) guide Piwi argonautes to their transposon targets for silencing. The highly conserved protein Maelstrom is linked to both piRNA biogenesis and effector roles in this pathway. One defining feature of Maelstrom is the predicted MAEL domain of unknown molecular function. Here, we present the first crystal structure of the MAEL domain from Bombyx Maelstrom, which reveals a nuclease fold. The overall architecture resembles that found in Mg(2+)- or Mn(2+)-dependent DEDD nucleases, but a clear distinguishing feature is the presence of a structural Zn(2+) ion coordinated by the conserved ECHC residues. Strikingly, metazoan Maelstrom orthologs across the animal kingdom lack the catalytic DEDD residues, and as we show for Bombyx Maelstrom are inactive as nucleases. However, a MAEL domain-containing protein from amoeba having both sequence motifs (DEDD and ECHC) is robustly active as an exoribonuclease. Finally, we show that the MAEL domain of Bombyx Maelstrom displays a strong affinity for single-stranded RNAs. Our studies suggest that the ancient MAEL nuclease domain evolved to function as an RNA-binding module in metazoan Maelstrom.

Indexed as

Evolution, MolecularAmino Acid SequenceAnimalsBombyxCrystallography, X-RayDrosophila ProteinsInsect ProteinsModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRibonucleasesRNA-Binding ProteinsRNA, Small InterferingSequence HomologyDrosophila ProteinsInsect Proteinsmael protein, DrosophilaRibonucleasesRNA-Binding ProteinsRNA, Small InterferingBombyxEHI_192630E. histolyticaMAELpiRNAPiwiribonuclease

Identifiers

PMID25778731
PMCPMC4408791
OpenAlexW2040176765

What OpenQuestion holds

Textmetadata
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.