Evidence map›Paper›PMID 28092367›Full record

ArticleNature structural & molecular biology2017

Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.

Franziska Theresia Edelmann, Andreas Schlundt, Roland Gerhard Heym, Andreas Jenner, Annika Niedner-Boblenz, Muhammad Ibrahim Syed, Jean-Christophe Paillart, Ralf Stehle, Robert Janowski, Michael Sattler and 2 more

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

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  11. mRNA Localization to the Endoplasmic Reticulum in Plant Endosperm Cells.International journal of molecular sciences · 2022
    Review
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  15. Intracellular mRNA transport and localized translation.Nature reviews. Molecular cell biology · 2021
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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 5 institutions in 2 countries.

Franziska Theresia EdelmannInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
Andreas SchlundtCenter for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
Roland Gerhard HeymInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
Andreas JennerInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Annika Niedner-BoblenzBiomedical Center of the Ludwig-Maximilians-Universität München, Department of Cell Biology, Planegg-Martinsried, Germany.
Muhammad Ibrahim SyedInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Jean-Christophe PaillartArchitecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.ORCID 0000-0003-1647-8917
Ralf StehleCenter for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
Robert JanowskiInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
Michael SattlerInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
Ralf-Peter JansenInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
Dierk NiessingInstitute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.ORCID 0000-0002-5589-369X
Helmholtz Zentrum München · DECenter for Integrated Protein Science Munich · DEUniversity of Tübingen · DEArchitecture et Réactivité de l'arN · FRBernstein Center for Computational Neuroscience Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex.

Indexed as

Base SequenceBinding SitesCrystallography, X-RayHydrogen BondingInverted Repeat SequencesModels, MolecularProtein BindingRepressor ProteinsRNA-Binding ProteinsRNA, MessengerRNA TransportSaccharomyces cerevisiae ProteinsASH1 protein, S cerevisiaeRepressor ProteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSHE2 protein, S cerevisiaeSHE3 protein, S cerevisiae

Identifiers

PMID28092367
OpenAlexW2572952976

What OpenQuestion holds

Textmetadata
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.