Evidence map›Paper›PMID 25497230›Full record

ArticleeLife2014

Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase.

Anna L Mallam, David J Sidote, Alan M Lambowitz

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Substrate Specificities of DDX1: A Human DEAD-box protein.bioRxiv : the preprint server for biology · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
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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

3 authors at 1 institution in 1 country.

Anna L MallamInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, United States.
David J SidoteInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, United States.
Alan M LambowitzInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, United States.
The University of Texas at Austin · US

Funding

RNA SPLICING IN NEUROSPORA MITOCHONDRIAR01GM037951 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI LAMBOWITZ, ALAN M. · 1986 to 2016
$6.6M
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 R37 GM037951
6 · The paper itself

Abstract

How different helicase families with a conserved catalytic 'helicase core' evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear. In this study, we used Mss116, a yeast DEAD-box protein that utilizes ATP to locally unwind dsRNA, to investigate helicase specificity and mechanism. Our results define the molecular basis for the substrate specificity of a DEAD-box protein. Additionally, they show that Mss116 has ambiguous substrate-binding properties and interacts with all four NTPs and both RNA and DNA. The efficiency of unwinding correlates with the stability of the 'closed-state' helicase core, a complex with nucleotide and nucleic acid that forms as duplexes are unwound. Crystal structures reveal that core stability is modulated by family-specific interactions that favor certain substrates. This suggests how present-day helicases diversified from an ancestral core with broad specificity by retaining core closure as a common catalytic mechanism while optimizing substrate-binding interactions for different cellular functions.

Indexed as

Evolution, MolecularBase SequenceBinding SitesBiocatalysisCrystallography, X-RayDEAD-box RNA HelicasesDNA, FungalEscherichia coliGene ExpressionModels, MolecularMolecular Sequence DataNucleic Acid ConformationOligonucleotidesProtein BindingProtein Structure, SecondaryRecombinant ProteinsDEAD-box RNA HelicasesDNA, FungalMSS116 protein, S cerevisiaeOligonucleotidesRecombinant ProteinsRNA, FungalSaccharomyces cerevisiae ProteinsbiochemistrybiophysicsDEAD-box proteinenzyme mechanismenzyme specificitymolecular evolutionRNA helicaseRNA unwindingS. cerevisiaestructural biology

Identifiers

PMID25497230
PMCPMC4383044
OpenAlexW2138574325

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.