Evidence map›Paper›PMID 28059701›Full record

ArticleeLife2017

Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1.

Yi Ren, Philip Schmiege, Günter Blobel

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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

3 authors.

Yi RenLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, United States.
Philip SchmiegeLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, United States.
Günter BlobelLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, United States.ORCID 0000-0002-7839-8341

Funding

RES FACIL CONSTRUCTION: HALLUCINOGENSC06RR017528 · NCRR · NEW YORK STRUCTURAL BIOLOGY CENTER · PI COWBURN, DAVID · 2002 to 2002
$2.0M
NCRR NIH HHS C06 RR017528
6 · The paper itself

Abstract

mRNA is cotranscrptionally processed and packaged into messenger ribonucleoprotein particles (mRNPs) in the nucleus. Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions. In yeast, one of these reactions involves loading of the mRNA-binding protein Yra1 by the DEAD-box ATPase Sub2 as assisted by the hetero-pentameric THO complex. To obtain molecular insights into reaction mechanisms, we determined crystal structures of two relevant complexes: a THO hetero-pentamer bound to Sub2 at 6.0 Å resolution; and Sub2 associated with an ATP analogue, RNA, and a C-terminal fragment of Yra1 (Yra1-C) at 2.6 Å resolution. We found that the 25 nm long THO clamps Sub2 in a half-open configuration; in contrast, when bound to the ATP analogue, RNA and Yra1-C, Sub2 assumes a closed conformation. Both THO and Yra1-C stimulated Sub2's intrinsic ATPase activity. We propose that THO surveys common landmarks in each nuclear mRNP to localize Sub2 for targeted loading of Yra1.

Indexed as

Adenosine TriphosphatasesCrystallography, X-RayModels, MolecularNuclear ProteinsProtein ConformationRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine Triphosphatasesmessenger ribonucleoproteinNuclear ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA-dependent ATPaseSaccharomyces cerevisiae ProteinsTHO2 protein, S cerevisiaeTranscription FactorsYRA1 protein, S cerevisiaebiochemistrybiophysicsDEAD-box ATPasemRNP remodelingS. cerevisiaestructural biologyX-ray crystallography

Identifiers

PMID28059701
PMCPMC5218534

What OpenQuestion holds

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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.