Evidence map›Paper›PMID 37935663›Full record

ArticleNature communications2023

RNA recognition by Npl3p reveals U2 snRNA-binding compatible with a chaperone role during splicing.

Ahmed Moursy, Antoine Cléry, Stefan Gerhardy, Katharina M Betz, Sanjana Rao, Jarosław Mazur, Sébastien Campagne, Irene Beusch, Malgorzata M Duszczyk, Mark D Robinson and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. 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
0.9field-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, 6 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 5 institutions in 3 countries.

Ahmed Moursy *Department of Biology, Institute of Biochemistry, ETH Zurich, Switzerland.
Antoine Cléry *Department of Biology, Institute of Biochemistry, ETH Zurich, Switzerland. antoine.clery@bc.biol.ethz.ch.ORCID 0000-0002-4550-6908
Stefan GerhardyDepartment of Biology, Institute of Biochemistry, ETH Zurich, Switzerland.ORCID 0000-0003-1826-5907
Katharina M BetzInstitute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.ORCID 0000-0001-5041-6205
Sanjana RaoInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
Jarosław MazurInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-1677-011X
Sébastien CampagneDepartment of Biology, Institute of Biochemistry, ETH Zurich, Switzerland.
Irene BeuschDepartment of Biology, Institute of Biochemistry, ETH Zurich, Switzerland.ORCID 0000-0001-7758-4348
Malgorzata M DuszczykDepartment of Biology, Institute of Biochemistry, ETH Zurich, Switzerland.
Mark D RobinsonInstitute of Molecular Life Sciences, University of Zurich, Zurich, Switzerland.ORCID 0000-0002-3048-5518
Vikram Govind PanseInstitute of Medical Microbiology, University of Zurich, Zurich, Switzerland. vpanse@imm.uzh.ch.ORCID 0000-0002-4770-7068
Frédéric H-T AllainDepartment of Biology, Institute of Biochemistry, ETH Zurich, Switzerland. allain@bc.biol.ethz.ch.ORCID 0000-0002-2131-6237
University of Zurich · CHETH Zurich · CHNovartis (Switzerland) · CHUniversité de Bordeaux · FRUniversity of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved SR-like protein Npl3 promotes splicing of diverse pre-mRNAs. However, the RNA sequence(s) recognized by the RNA Recognition Motifs (RRM1 & RRM2) of Npl3 during the splicing reaction remain elusive. Here, we developed a split-iCRAC approach in yeast to uncover the consensus sequence bound to each RRM. High-resolution NMR structures show that RRM2 recognizes a 5´-GNGG-3´ motif leading to an unusual mille-feuille topology. These structures also reveal how RRM1 preferentially interacts with a CC-dinucleotide upstream of this motif, and how the inter-RRM linker and the region C-terminal to RRM2 contribute to cooperative RNA-binding. Structure-guided functional studies show that Npl3 genetically interacts with U2 snRNP specific factors and we provide evidence that Npl3 melts U2 snRNA stem-loop I, a prerequisite for U2/U6 duplex formation within the catalytic center of the B

Indexed as

RNARNA SplicingNuclear ProteinsNucleic Acid ConformationRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesNPL3 protein, S cerevisiaeNuclear ProteinsRibonucleoprotein, U2 Small NuclearRNARNA-Binding ProteinsRNA, Small NuclearSaccharomyces cerevisiae ProteinsU2 small nuclear RNA

Identifiers

PMID37935663
PMCPMC10630445
OpenAlexW4388464768

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.