Evidence map›Paper›PMID 33883550›Full record

ArticleNature communications2021

RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment.

Pallabi Basu, Maya Elgrably-Weiss, Fouad Hassouna, Manoj Kumar, Reuven Wiener, Shoshy Altuvia

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. An acetyltranferase moonlights as a regulator of the RNA binding repertoire of the RNA chaperone Hfq inProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. 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

6 authors at 1 institution in 1 country.

Pallabi BasuDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel.ORCID http://orcid.org/0000-0002-8163-7518
Maya Elgrably-WeissDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel.ORCID http://orcid.org/0000-0001-7939-0774
Fouad HassounaDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel.
Manoj KumarDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel.
Reuven WienerDepartment of Biochemistry and Molecular Biology, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel.
Shoshy AltuviaDepartment of Microbiology and Molecular Genetics, IMRIC, The Hebrew University, Hadassah Medical School, Jerusalem, Israel. shoshy.altuvia@mail.huji.ac.il.
Hebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA chaperone Hfq, acting as a hexamer, is a known mediator of post-transcriptional regulation, expediting basepairing between small RNAs (sRNAs) and their target mRNAs. However, the intricate details associated with Hfq-RNA biogenesis are still unclear. Previously, we reported that the stringent response regulator, RelA, is a functional partner of Hfq that facilitates Hfq-mediated sRNA-mRNA regulation in vivo and induces Hfq hexamerization in vitro. Here we show that RelA-mediated Hfq hexamerization requires an initial binding of RNA, preferably sRNA to Hfq monomers. By interacting with a Shine-Dalgarno-like sequence (GGAG) in the sRNA, RelA stabilizes the initially unstable complex of RNA bound-Hfq monomer, enabling the attachment of more Hfq subunits to form a functional hexamer. Overall, our study showing that RNA binding to Hfq monomers is at the heart of RelA-mediated Hfq hexamerization, challenges the previous concept that only Hfq hexamers can bind RNA.

Indexed as

Amino Acid SubstitutionBase SequenceEscherichia coliEscherichia coli ProteinsGTP PyrophosphokinaseHost Factor 1 ProteinModels, BiologicalProtein BindingProtein MultimerizationProtein StabilityProtein Structure, QuaternaryProtein SubunitsRNA, BacterialRNA, Small UntranslatedSequence DeletionTranscription Factor RelAEscherichia coli ProteinsGTP PyrophosphokinaseHfq protein, E coliHost Factor 1 ProteinProtein SubunitsrelA protein, E coliRNA, BacterialRNA, Small UntranslatedTranscription Factor RelA

Identifiers

PMID33883550
PMCPMC8060364
OpenAlexW3154068806

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.