Evidence map›Paper›PMID 21746911›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail.

Anna L Mallam, Inga Jarmoskaite, Pilar Tijerina, Mark Del Campo, Soenke Seifert, Liang Guo, Rick Russell, Alan M Lambowitz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. TheRNA (New York, N.Y.) · 2020
    Article
  13. Review
  14. Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  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

8 authors at 4 institutions in 2 countries.

Anna L MallamDepartment of Chemistry and Biochemistry, University of Texas, Austin, TX 78712, USA.
Inga Jarmoskaite
Pilar Tijerina
Mark Del Campo
Soenke Seifert
Liang Guo
Rick Russell
Alan M Lambowitz
Institut de Biologie Moléculaire et Cellulaire · FRThe University of Texas at Austin · USArgonne National Laboratory · USIllinois Institute of Technology · US

Funding

RNA SPLICING IN NEUROSPORA MITOCHONDRIAR01GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2016
$6.6M
Physical and functional probing of DEAD-box proteins as general RNA chaperonesR01GM070456 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI RUSSELL, RICK · 2004 to 2017
$3.6M
INVOLVEMENT OF PROTEINS IN SPLICING GROUP I INTRONSR37GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1993 to 2002
$1.2M
NIGMS NIH HHS GM037951NIGMS NIH HHS R01 GM037951NIGMS NIH HHS R01 GM070456NIGMS NIH HHS R37 GM037951
6 · The paper itself

Abstract

The mitochondrial DEAD-box proteins Mss116p of Saccharomyces cerevisiae and CYT-19 of Neurospora crassa are ATP-dependent helicases that function as general RNA chaperones. The helicase core of each protein precedes a C-terminal extension and a basic tail, whose structural role is unclear. Here we used small-angle X-ray scattering to obtain solution structures of the full-length proteins and a series of deletion mutants. We find that the two core domains have a preferred relative orientation in the open state without substrates, and we visualize the transition to a compact closed state upon binding RNA and adenosine nucleotide. An analysis of complexes with large chimeric oligonucleotides shows that the basic tails of both proteins are attached flexibly, enabling them to bind rigid duplex DNA segments extending from the core in different directions. Our results indicate that the basic tails of DEAD-box proteins contribute to RNA-chaperone activity by binding nonspecifically to large RNA substrates and flexibly tethering the core for the unwinding of neighboring duplexes.

Indexed as

Binding SitesCircular DichroismDEAD-box RNA HelicasesFungal ProteinsModels, MolecularNeurospora crassaNucleic Acid ConformationProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsScattering, Small AngleStructural Homology, ProteinDEAD-box RNA HelicasesFungal ProteinsMSS116 protein, S cerevisiaeRecombinant ProteinsRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID21746911
PMCPMC3145681
OpenAlexW2076355407

What OpenQuestion holds

Textmetadata
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.