Evidence map›Paper›PMID 22745434›Full record

ArticleScience (New York, N.Y.)2012

Elastic coupling between RNA degradation and unwinding by an exoribonuclease.

Gwangrog Lee, Matthew A Bratkowski, Fang Ding, Ailong Ke, Taekjip Ha

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Opto-refrigerative tweezers.Science advances · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Substrate selectivity by the exonuclease Rrp6p.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Mimicking Co-Transcriptional RNA Folding Using a Superhelicase.Journal of the American Chemical Society · 2018
    Article
  17. NrnC, an RNase D-Like Protein FromFrontiers in microbiology · 2018
    Article
  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

5 authors at 3 institutions in 2 countries.

Gwangrog LeeDepartment of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, IL 61801, USA.
Matthew A Bratkowski
Fang Ding
Ailong Ke
Taekjip Ha
Cornell University · USGwangju Institute of Science and Technology · KRUniversity of Illinois Urbana-Champaign · US

Funding

Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
Structure and Function of S-adenosyl-L-methionine RiboswitchesR01GM086766 · NIGMS · CORNELL UNIVERSITY · PI KE, AILONG · 2010 to 2014
$1.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM065367NIGMS NIH HHS GM-086766NIGMS NIH HHS R01 GM065367NIGMS NIH HHS R01 GM086766
6 · The paper itself

Abstract

Rrp44 (Dis3) is a key catalytic subunit of the yeast exosome complex and can processively digest structured RNA one nucleotide at a time in the 3' to 5' direction. Its motor function is powered by the energy released from the hydrolytic nuclease reaction instead of adenosine triphosphate hydrolysis as in conventional helicases. Single-molecule fluorescence analysis revealed that instead of unwinding RNA in single base pair steps, Rrp44 accumulates the energy released by multiple single nucleotide step hydrolysis reactions until about four base pairs are unwound in a burst. Kinetic analyses showed that RNA unwinding, not cleavage or strand release, determines the overall RNA degradation rate and that the unwinding step size is determined by the nonlinear elasticity of the Rrp44/RNA complex, but not by duplex stability.

Indexed as

RNA StabilityBase PairingExoribonucleasesExosome Multienzyme Ribonuclease ComplexRNA, FungalSaccharomyces cerevisiae ProteinsDIS3 protein, S cerevisiaeExoribonucleasesExosome Multienzyme Ribonuclease ComplexRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID22745434
PMCPMC3565423
OpenAlexW2014000161

What OpenQuestion holds

Textmetadata
LicenceTDM
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.