Evidence map›Paper›PMID 34157309›Full record

ArticleMolecular cell2021

A cooperative PNPase-Hfq-RNA carrier complex facilitates bacterial riboregulation.

Tom Dendooven, Dhriti Sinha, Alzbeta Roeselová, Todd A Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J Bandyra

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-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

34 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Journal of molecular biology · 2026
    Article
  3. Structural insights into RNA recognition by theProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. What makes a small RNA work?Nucleic acids research · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 2 institutions in 2 countries.

Tom DendoovenDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Dhriti SinhaDepartment of Microbiology & Molecular Genetics, University of Texas Health Science Center, 6431 Fannin Street, MSE R266, Houston, TX 77030, USA.
Alzbeta RoeselováDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
Todd A CameronDepartment of Microbiology & Molecular Genetics, University of Texas Health Science Center, 6431 Fannin Street, MSE R266, Houston, TX 77030, USA.
Nicholas R De LayDepartment of Microbiology & Molecular Genetics, University of Texas Health Science Center, 6431 Fannin Street, MSE R266, Houston, TX 77030, USA.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK. Electronic address: bfl20@cam.ac.uk.
Katarzyna J BandyraDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK. Electronic address: kjb69@cam.ac.uk.
University of Cambridge · GBThe University of Texas Health Science Center at Houston · US

Funding

Systematic Analysis Of Small RNA-Based Regulation Of Gene Expression In BacteriaR01GM121368 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DE LAY, NICHOLAS R. · 2017 to 2021
$1.7M
NIGMS NIH HHS R01 GM121368Wellcome Trust 200873/Z/16/Z
6 · The paper itself

Abstract

Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic consequences for gene regulation. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq, and sRNA and show that this complex boosts sRNA stability in vitro. Comparison of structures for PNPase in RNA carrier and degradation modes reveals how the RNA is rerouted away from the active site through interactions with Hfq and the KH and S1 domains. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E and could aid RNA presentation to facilitate regulatory actions on target genes.

Indexed as

Catalytic DomainEndoribonucleasesEscherichia coliEscherichia coli ProteinsExoribonucleasesGene Expression Regulation, BacterialHost Factor 1 ProteinMolecular ChaperonesPolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA, Small UntranslatedRNA StabilityEndoribonucleasesEscherichia coli ProteinsExoribonucleasesHfq protein, E coliHost Factor 1 ProteinMolecular ChaperonesPolyribonucleotide Nucleotidyltransferaseribonuclease ERNA, BacterialRNA, Small UntranslatedcryoEMgene silencingHfqpolynucleotide phosphorylaseribonucleaseribonucleoprotein complexriboregulationRNA chaperonesmall regulatory RNA

Identifiers

PMID34157309
PMCPMC8294330
OpenAlexW3177119683

What OpenQuestion holds

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LicenceCC BY
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.