Evidence map›Paper›PMID 28180315›Full record

ArticleNucleic acids research2017

Structural basis for the dimerization of Nab2 generated by RNA binding provides insight into its contribution to both poly(A) tail length determination and transcript compaction in Saccharomyces cerevisiae.

Shintaro Aibara, James M B Gordon, Anja S Riesterer, Stephen H McLaughlin, Murray Stewart

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. The Great Escape: mRNA Export through the Nuclear Pore Complex.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Polyadenylation and nuclear export of mRNAs.The Journal of biological chemistry · 2019
    Review
  17. Molecular basis for the recognition of the human AAUAAA polyadenylation signal.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Integration of mRNP formation and export.Cellular and molecular life sciences : CMLS · 2017
    Review
  20. 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 1 institution in 1 country.

Shintaro AibaraMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
James M B GordonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
Anja S RiestererMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
Stephen H McLaughlinMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
Murray StewartMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge, UK
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178939
6 · The paper itself

Abstract

In Saccharomyces cerevisiae generation of export-competent mRNPs terminates the nuclear phase of the gene expression pathway and facilitates transport to the cytoplasm for translation. Nab2 functions in this process to control both mRNP compaction that facilitates movement through nuclear pore complexes and the length of transcript poly(A) tails. Nab2 has a modular structure that includes seven CCCH Zn fingers that bind to A-rich RNAs and fingers 5–7 are critical for these functions. Here, we demonstrate, using both biophysical and structural methods, that binding A11G RNA induces dimerization of Zn fingers 5–7 mediated by the novel spatial arrangement of the fingers promoting each RNA chain binding two protein chains. The dimerization of Nab2 induced by RNA binding provides a basis for understanding its function in both poly(A) tail length regulation and in the compaction of mature transcripts to facilitate nuclear export.

Indexed as

Active Transport, Cell NucleusAmino Acid SubstitutionBase SequenceBiophysical PhenomenaCrystallography, X-RayGalactokinaseGenes, FungalModels, MolecularMutagenesis, Site-DirectedNucleocytoplasmic Transport ProteinsPolyadenylationProtein DomainsProtein MultimerizationRecombinant ProteinsRNA-Binding ProteinsRNA, FungalGAL1 protein, S cerevisiaeGalactokinaseNAB2 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsRecombinant ProteinsRNA-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID28180315
PMCPMC5388407
OpenAlexW2563894372

What OpenQuestion holds

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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.