Evidence map›Paper›PMID 26602689›Full record

ArticleNucleic acids research2016

Gbp2 interacts with THO/TREX through a novel type of RRM domain.

Santiago Martínez-Lumbreras, Valerio Taverniti, Silvia Zorrilla, Bertrand Séraphin, José Manuel Pérez-Cañadillas

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. The serine-arginine (SR) protein UmRrm75 from Ustilago maydis is a functional ortholog of yeast ScHrb1.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Frontiers in cellular and infection microbiology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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

5 authors at 2 institutions in 2 countries.

Santiago Martínez-LumbrerasDepartment of Biological Physical Chemistry, Instituto de Química-Física 'Rocasolano', CSIC, Serrano-119, 28006 Madrid, Spain.
Valerio TavernitiEquipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGMBC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France.
Silvia ZorrillaDepartment of Cellular and Molecular Biology, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Bertrand SéraphinEquipe Labellisée La Ligue, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGMBC), Centre National de Recherche Scientifique (CNRS) UMR 7104/Institut National de Santé et de Recherche Médicale (INSERM) U964/Université de Strasbourg, 67404 Illkirch, France seraphin@igbmc.fr.
José Manuel Pérez-CañadillasDepartment of Biological Physical Chemistry, Instituto de Química-Física 'Rocasolano', CSIC, Serrano-119, 28006 Madrid, Spain jmperez@iqfr.csic.es.
Institut de Biologie Moléculaire et Cellulaire · FRCentro de Investigaciones Biológicas Margarita Salas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metazoan SR and SR-like proteins are important regulatory factors in RNA splicing, export, translation and RNA decay. We determined the NMR structures and nucleic acid interaction modes of Gbp2 and Hrb1, two paralogous budding yeast proteins with similarities to mammalian SR proteins. Gbp2 RRM1 and RRM2 recognise preferentially RNAs containing the core motif GGUG. Sequence selectivity resides in a non-canonical interface in RRM2 that is highly related to the SRSF1 pseudoRRM. The atypical Gbp2/Hrb1 C-terminal RRM domains (RRM3) do not interact with RNA/DNA, likely because of their novel N-terminal extensions that block the canonical RNA binding interface. Instead, we discovered that RRM3 is crucial for interaction with the THO/TREX complex and identified key residues essential for this interaction. Moreover, Gbp2 interacts genetically with Tho2 as the double deletion shows a synthetic phenotype and preventing Gbp2 interaction with the THO/TREX complex partly supresses gene expression defect associated with inactivation of the latter complex. These findings provide structural and functional insights into the contribution of SR-like proteins in the post-transcriptional control of gene expression.

Indexed as

Protein Interaction Domains and MotifsCarbon-13 Magnetic Resonance SpectroscopyDNAModels, MolecularMultiprotein ComplexesNucleocytoplasmic Transport ProteinsPoly(A)-Binding ProteinsProtein BindingProtein ConformationProton Magnetic Resonance SpectroscopyRNARNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTelomereDNAGbp2 protein, S cerevisiaeHrb1 protein, S cerevisiaeMultiprotein ComplexesNucleocytoplasmic Transport ProteinsPoly(A)-Binding ProteinsRNARNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID26602689
PMCPMC4705658
OpenAlexW2174375643

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.