Evidence map›Paper›PMID 25218446›Full record

ArticleNature structural & molecular biology2014

Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.

Piotr Wysoczański, Cornelius Schneider, ShengQi Xiang, Francesca Munari, Simon Trowitzsch, Markus C Wahl, Reinhard Lührmann, Stefan Becker, Markus Zweckstetter

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

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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

9 authors.

Piotr WysoczańskiDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Cornelius SchneiderDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
ShengQi XiangDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Francesca MunariDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Simon Trowitzsch1] Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. [2].ORCID 000000019143766X
Markus C WahlLaboratory of Structural Biochemistry, Freie Universität Berlin, Berlin, Germany.
Reinhard LührmannDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Stefan BeckerDepartment for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Markus Zweckstetter1] Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. [2] German Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany. [3] Center for Nanoscale Microscopy and Molecular Physiology of the Brain, University Medical Center, Göttingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The precursor mRNA (pre-mRNA) retention and splicing (RES) complex is a spliceosomal complex that is present in yeast and humans and is important for RNA splicing and retention of unspliced pre-mRNA. Here, we present the solution NMR structure of the RES core complex from Saccharomyces cerevisiae. Complex formation leads to an intricate folding of three components-Snu17p, Bud13p and Pml1p-that stabilizes the RNA-recognition motif (RRM) fold of Snu17p and increases binding affinity in tertiary interactions between the components by more than 100-fold compared to that in binary interactions. RES interacts with pre-mRNA within the spliceosome, and through the assembly of the RES core complex RNA binding efficiency is increased. The three-dimensional structure of the RES core complex highlights the importance of cooperative folding and binding in the functional organization of the spliceosome.

Indexed as

Carrier ProteinsNucleic Acid ConformationRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, FungalRNA PrecursorsRNA SplicingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesBUD13 homolog protein, humanBud13 protein, S cerevisiaeCarrier ProteinsIST3 protein, S cerevisiaePml1 protein, S cerevisiaeRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, FungalRNA PrecursorsSaccharomyces cerevisiae Proteins

Identifiers

PMID25218446

What OpenQuestion holds

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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.