Evidence map›Paper›PMID 31104083›Full record

ReviewCurrent genetics2019

New molecular interactions broaden the functions of the RNA chaperone Hfq.

Ricardo F Dos Santos, Cecília M Arraiano, José M Andrade

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.1field-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

36 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  5. Review
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  8. Review
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  12. Interactions and Insertion ofInternational journal of molecular sciences · 2023
    Article
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  19. Article
  20. Molecular mechanism of enhanced ethanol tolerance associated withFrontiers in bioengineering and biotechnology · 2022
    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

3 authors at 1 institution in 1 country.

Ricardo F Dos SantosInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157, Oeiras, Portugal.
Cecília M ArraianoInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157, Oeiras, Portugal. cecilia@itqb.unl.pt.ORCID http://orcid.org/0000-0003-1934-9301
José M AndradeInstituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157, Oeiras, Portugal. andrade@itqb.unl.pt.
Universidade Nova de Lisboa · PT

Funding

NCI PHYSICIAN-INVESTIGATOR DEVELOPMENT AWARD PROGRAMK08CA000961 · NCI · ROCKEFELLER UNIVERSITY · PI YOUNG, JAMES W. · 1985 to 1991
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FCT - Fundação para a Ciência e a Tecnologia (Portugal) IF/00961/2014FCT - Fundação para a Ciência e a Tecnologia (Portugal) PTDC/BIA-MIC/1399/2014FCT - Fundação para a Ciência e a Tecnologia (Portugal) PTDC/BIA-MIC/32525/2017FCT - Fundação para a Ciência e a Tecnologia (Portugal) PTDC/IMI-MIC/4463/2014FEDER through COMPETE2020 - Programa Operacional Competitividade e Internacionalização (POCI) Estrutural e Celular)FEDER through COMPETE2020 - Programa Operacional Competitividade e Internacionalização (POCI) Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular
6 · The paper itself

Abstract

The RNA chaperone Hfq is an important bacterial post-transcriptional regulator. Most studies on Hfq are focused on the role of this protein on small non-coding RNAs (sRNAs) and messenger RNAs (mRNAs). The most well-characterized function of Hfq is its role as RNA matchmaker, promoting the base-pairing between sRNAs and their mRNA targets. However, novel substrates and previous unrecognized functions of Hfq have now been identified, which expanded the regulatory spectrum of this protein. Hfq was recently found to bind rRNA and act as a new ribosome biogenesis factor, affecting rRNA processing, ribosome assembly, translational efficiency and translational fidelity. Hfq was also found to bind tRNAs, which could provide an additional mechanism for its role on the accuracy of protein synthesis. The list of substrates does not include RNA exclusively since Hfq was shown to bind DNA, playing an important role in DNA compaction. Additionally, Hfq is also capable to establish many protein-protein interactions. Overall, the functions of the RNA-binding protein Hfq have been expanded beyond its function in small RNA-mediated regulation. The identification of additional substrates and new functions provides alternative explanations for the importance of the chaperone Hfq as a global regulator.

Indexed as

DNAEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHost Factor 1 ProteinMolecular ChaperonesProtein BiosynthesisRNA-Binding ProteinsRNA, MessengerRNA Processing, Post-TranscriptionalRNA, RibosomalRNA, Small UntranslatedRNA, TransferDNAEscherichia coli ProteinsHfq protein, E coliHost Factor 1 ProteinMolecular ChaperonesRNA-Binding ProteinsRNA, MessengerRNA, RibosomalRNA, Small UntranslatedRNA, TransferDNAHfqLsm familymRNAPost-transcriptional regulationrRNAsRNAtRNA

Identifiers

PMID31104083
OpenAlexW2945815787

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.