Evidence map›Paper›PMID 29036353›Full record

ArticleNucleic acids research2017

Structural insights into RNA unwinding and degradation by RNase R.

Lee-Ya Chu, Tung-Ju Hsieh, Bagher Golzarroshan, Yi-Ping Chen, Sashank Agrawal, Hanna S Yuan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. 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
2.9field-weighted citation impact, top 9% 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, 46 citations in OpenAlex.

  1. HELZ2 RegulatesCirculation · 2026
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  6. Review
  7. Article
  8. Article
  9. Exoribonuclease RNase R protects AntarcticApplied and environmental microbiology · 2023
    Article
  10. Article
  11. A shape-shifting nuclease unravels structured RNA.Nature structural & molecular biology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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  20. Review
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

6 authors at 1 institution in 1 country.

Lee-Ya ChuInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Tung-Ju HsiehInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Bagher GolzarroshanInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Yi-Ping ChenInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Sashank AgrawalInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Hanna S YuanInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, ROC.
Institute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNase R is a conserved exoribonuclease in the RNase II family that primarily participates in RNA decay in all kingdoms of life. RNase R degrades duplex RNA with a 3' overhang, suggesting that it has RNA unwinding activity in addition to its 3'-to-5' exoribonuclease activity. However, how RNase R coordinates RNA binding with unwinding to degrade RNA remains elusive. Here, we report the crystal structure of a truncated form of Escherichia coli RNase R (residues 87-725) at a resolution of 1.85 Å. Structural comparisons with other RNase II family proteins reveal two open RNA-binding channels in RNase R and suggest a tri-helix 'wedge' region in the RNB domain that may induce RNA unwinding. We constructed two tri-helix wedge mutants and they indeed lost their RNA unwinding but not RNA binding or degrading activities. Our results suggest that the duplex RNA with an overhang is bound in the two RNA-binding channels in RNase R. The 3' overhang is threaded into the active site and the duplex RNA is unwound upon reaching the wedge region during RNA degradation. Thus, RNase R is a proficient enzyme, capable of concurrently binding, unwinding and degrading structured RNA in a highly processive manner during RNA decay.

Indexed as

Nucleic Acid ConformationProtein DomainsBiocatalysisCatalytic DomainCrystallography, X-RayEscherichia coli ProteinsExoribonucleasesKineticsModels, MolecularMutationProtein BindingRNA, BacterialRNA CleavageRNA StabilityEscherichia coli ProteinsExoribonucleasesribonuclease RRNA, Bacterial

Identifiers

PMID29036353
PMCPMC5714204
OpenAlexW2761493852

What OpenQuestion holds

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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.