Evidence map›Paper›PMID 28370625›Full record

ReviewMolecular microbiology2017

ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?

Mikolaj Olejniczak, Gisela Storz

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
7.8field-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

90 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
  2. Article
  3. Molecular genetic characterization of bacterial KH-domain proteins.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. What makes a small RNA work?Nucleic acids research · 2025
    Review
  8. Unexpected Richness of the Bacterial Small RNA World.Journal of molecular biology · 2025
    Review
  9. Article
  10. RNA recognition by minimal ProQ fromRNA (New York, N.Y.) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Broadly conserved FlgV controls flagellar assembly andbioRxiv : the preprint server for biology · 2024
    Article

30 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 2 countries.

Mikolaj OlejniczakInstitute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, Poznan, 61-614, Poland.
Gisela StorzDivision of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institutes of Child Health and Human Development, Bethesda, MD, 20892-4417, USA.ORCID http://orcid.org/0000-0001-6698-1241
Adam Mickiewicz University in Poznań · PLEunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Small Regulatory RNAsZIAHD001608 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STORZ, GISELA · 2009 to 2025
$16.9M
Intramural NIH HHS ZIA HD001608
6 · The paper itself

Abstract

Small RNAs (sRNAs), particularly those that act by limited base pairing with mRNAs, are part of most regulatory networks in bacteria. In many cases, the base-pairing interaction is facilitated by the RNA chaperone Hfq. However, not all bacteria encode Hfq and some base-pairing sRNAs do not require Hfq raising the possibility of other RNA chaperones. Candidates are proteins with homology to FinO, a factor that promotes base pairing between the FinP antisense sRNA and the traJ mRNA to control F plasmid transfer. Recent papers have shown that the Salmonella enterica FinO-domain protein ProQ binds a large suite of sRNAs, including the RaiZ sRNA, which represses translation of the hupA mRNA, and the Legionella pneumophila protein RocC binds the RocR sRNA, which blocks expression of competence genes. Here we discuss what is known about FinO-domain structures, including the recently solved Escherichia coli ProQ structure, as well as the RNA binding properties of this family of proteins and evidence they act as chaperones. We compare these properties with those of Hfq. We further summarize what is known about the physiological roles of FinO-domain proteins and enumerate outstanding questions whose answers will establish whether they constitute a second major class of RNA chaperones.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsConserved SequenceEscherichia coliEscherichia coli ProteinsF FactorMolecular ChaperonesNucleic Acid ConformationProtein DomainsRepressor ProteinsRNA, AntisenseRNA, BacterialRNA-Binding ProteinsRNA, MessengerStructure-Activity RelationshipBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsFinO protein, E coliMolecular ChaperonesProQ protein, E coliRepressor ProteinsRNA, AntisenseRNA, BacterialRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID28370625
PMCPMC5578414
OpenAlexW2600679317

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.