Evidence map›Paper›PMID 26759452›Full record

ArticleRNA (New York, N.Y.)2016

The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.

Katarzyna J Bandyra, Dhriti Sinha, Johanna Syrjanen, Ben F Luisi, Nicholas R De Lay

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
10.8field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. CsrA Shows Selective Regulation of sRNA-mRNA Networks.bioRxiv : the preprint server for biology · 2023
    Article
  9. Target recognition by RNase E RNA-binding domain AR2 drives sRNA decay in the absence of PNPase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Regulation of mRNA decay inCritical reviews in biochemistry and molecular biology · 2022
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

5 authors at 2 institutions in 2 countries.

Katarzyna J BandyraDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
Dhriti SinhaDepartment of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030, USA.
Johanna SyrjanenDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
Nicholas R De LayDepartment of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, Texas 77030, USA Graduate School of Biomedical Sciences, University of Texas Health Science Center, Houston, Texas 77030, USA.
University of Cambridge · GBThe University of Texas at Austin · US

Funding

Intramural NIH HHSWellcome Trust 076846Wellcome Trust 076846/Z/05/AWellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

In all bacterial species examined thus far, small regulatory RNAs (sRNAs) contribute to intricate patterns of dynamic genetic regulation. Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein, but genetic screens have also recently identified the 3'-to-5' exoribonuclease polynucleotide phosphorylase (PNPase) as an unexpected stabilizer and facilitator of sRNAs in vivo. To understand how a ribonuclease might mediate these effects, we tested the interactions of PNPase with sRNAs and found that the enzyme can readily degrade these nucleic acids in vitro but, nonetheless, copurifies from cell extracts with the same sRNAs without discernible degradation or modification to their 3' ends, suggesting that the associated RNA is protected against the destructive activity of the ribonuclease. In vitro, PNPase, Hfq, and sRNA can form a ternary complex in which the ribonuclease plays a nondestructive, structural role. Such ternary complexes might be formed transiently in vivo, but could help to stabilize particular sRNAs and remodel their population on Hfq. Taken together, our results indicate that PNPase can be programmed to act on RNA in either destructive or stabilizing modes in vivo and may form complex, protective ribonucleoprotein assemblies that shape the landscape of sRNAs available for action.

Indexed as

HydrolysisPolyribonucleotide NucleotidyltransferaseProtein BindingRNAPolyribonucleotide NucleotidyltransferaseRNAHfqpolynucleotide phosphorylaseRNA degradationRNase Esmall regulatory RNA

Identifiers

PMID26759452
PMCPMC4748814
OpenAlexW2239702807

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.