Evidence map›Paper›PMID 26872969›Full record

ArticleThe Journal of biological chemistry2016

How RNase R Degrades Structured RNA: ROLE OF THE HELICASE ACTIVITY AND THE S1 DOMAIN.

Sk Tofajjen Hossain, Arun Malhotra, Murray P Deutscher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 53 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. RNA exoribonucleases in E. coli.Archives of microbiology · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
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  15. Article
  16. Review
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Sk Tofajjen HossainFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101.
Arun MalhotraFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101.
Murray P DeutscherFrom the Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33101 m.deutscher@med.miami.edu.
University of Miami · US

Funding

RNases and RNA Metabolism in BacteriaR01GM016317 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI DEUTSCHER, MURRAY P · 1985 to 2019
$9.1M
GTP BINDING PROTEIN ACTIVATORF32GM016317 · NIGMS · U.S. NATIONAL INST/CHILD HLTH/HUMAN DEV · PI OOI, CHEAN E · 1993 to 1995
–
NIGMS NIH HHS F32 GM016317NIGMS NIH HHS GM 16317NIGMS NIH HHS R01 GM016317
6 · The paper itself

Abstract

RNase R, a ubiquitous 3' exoribonuclease, plays an important role in many aspects of RNA metabolism. In contrast to other exoribonucleases, RNase R can efficiently degrade highly structured RNAs, but the mechanism by which this is accomplished has remained elusive. It is known that RNase R contains an unusual, intrinsic RNA helicase activity that facilitates degradation of duplex RNA, but how it stimulates the nuclease activity has also been unclear. Here, we have made use of specifically designed substrates to compare the nuclease and helicase activities of RNase R. We have also identified and mutated several residues in the S1 RNA-binding domain that are important for interacting with duplex RNA and have measured intrinsic tryptophan fluorescence to analyze the conformational changes that occur upon binding of structured RNA. Using these approaches, we have determined the relation of the RNA helicase, ATP binding, and nuclease activities of RNase R. This information has been combined with a structural analysis of RNase R, based on its homology to RNase II, whose structure has been determined, to develop a detailed model that explains how RNase R digests structured RNA and how this differs from its action on single-stranded RNA.

Indexed as

Adenosine TriphosphateEscherichia coliEscherichia coli ProteinsExoribonucleasesModels, MolecularNucleic Acid ConformationProtein Structure, TertiaryRNA, BacterialRNA HelicasesRNA StabilitySubstrate SpecificityAdenosine TriphosphateEscherichia coli ProteinsExoribonucleasesribonuclease RRNA, BacterialRNA HelicasesATPconformational changeduplex RNAEscherichia coli (E. coli)P-loop domainribonuclaseRNA degradationRNA helicase

Identifiers

PMID26872969
PMCPMC4824996
OpenAlexW2255502678

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.