Evidence map›Paper›PMID 20554854›Full record

ArticleNucleic acids research2010

Dual roles for the Mss116 cofactor during splicing of the ai5γ group II intron.

Nora Zingler, Amanda Solem, Anna Marie Pyle

Abstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. ACS chemical biology · 2023
    Article
  3. Article
  4. Molecular and cellular biology · 2021
    Article
  5. DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. RNA helicase proteins as chaperones and remodelers.Annual review of biochemistry · 2014
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. RNA helicases and remodeling proteins.Current opinion in chemical biology · 2011
    Review
  15. Article
  16. Article
  17. Emerging structural themes in large RNA molecules.Current opinion in structural biology · 2011
    Review
  18. Article
  19. DEAD-box proteins as RNA helicases and chaperones.Wiley interdisciplinary reviews. RNA
    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

3 authors.

Nora ZinglerDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Amanda Solem
Anna Marie Pyle

Funding

STUCTURE AND FUNCTION OF GROUP II INTRONSR01GM050313 · NIGMS · YALE UNIVERSITY · PI PYLE, ANNA MARIE · 1994 to 2016
$4.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01GM50313
6 · The paper itself

Abstract

The autocatalytic group II intron ai5γ from Saccharomyces cerevisiae self-splices under high-salt conditions in vitro, but requires the assistance of the DEAD-box protein Mss116 in vivo and under near-physiological conditions in vitro. Here, we show that Mss116 influences the folding mechanism in several ways. By comparing intron precursor RNAs with long (∼300 nt) and short (∼20 nt) exons, we observe that long exon sequences are a major obstacle for self-splicing in vitro. Kinetic analysis indicates that Mss116 not only mitigates the inhibitory effects of long exons, but also assists folding of the intron core. Moreover, a mutation in conserved Motif III that impairs unwinding activity (SAT → AAA) only affects the construct with long exons, suggesting helicase unwinding during exon unfolding, but not in intron folding. Strong parallels between Mss116 and the related protein Cyt-19 from Neurospora crassa suggest that these proteins form a subclass of DEAD-box proteins that possess a versatile repertoire of diverse activities for resolving the folding problems of large RNAs.

Indexed as

IntronsRNA SplicingDEAD-box RNA HelicasesExonsFungal ProteinsKineticsMutationNucleic Acid ConformationSaccharomyces cerevisiae ProteinsSaltsDEAD-box RNA HelicasesFungal ProteinsMSS116 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSalts

Identifiers

PMID20554854
PMCPMC2965245

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Registered trials

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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.