Evidence map›Paper›PMID 38057323›Full record

ArticleNature communications2023

Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease.

Alejandro Tejada-Arranz, Aleksei Lulla, Maxime Bouilloux-Lafont, Evelyne Turlin, Xue-Yuan Pei, Thibaut Douché, Mariette Matondo, Allison H Williams, Bertrand Raynal, Ben F Luisi and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
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  4. Review
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

11 authors at 4 institutions in 5 countries.

Alejandro Tejada-ArranzDépartement de Microbiologie, Unité Pathogenèse de Helicobacter, UMR CNRS 6047, Institut Pasteur, Paris, France.ORCID 0000-0002-8452-8245
Aleksei LullaDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1GA, UK.
Maxime Bouilloux-LafontDépartement de Microbiologie, Unité Pathogenèse de Helicobacter, UMR CNRS 6047, Institut Pasteur, Paris, France.ORCID 0000-0002-1145-9015
Evelyne TurlinDépartement de Microbiologie, Unité Pathogenèse de Helicobacter, UMR CNRS 6047, Institut Pasteur, Paris, France.
Xue-Yuan PeiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1GA, UK.ORCID 0000-0001-7083-9651
Thibaut DouchéPlateforme Protéomique, Unité de Spectrométrie de Masse pour la Biologie, C2RT, USR CNRS 2000, Institut Pasteur, Paris, France.ORCID 0000-0001-8627-6726
Mariette MatondoPlateforme Protéomique, Unité de Spectrométrie de Masse pour la Biologie, C2RT, USR CNRS 2000, Institut Pasteur, Paris, France.ORCID 0000-0003-3958-7710
Allison H WilliamsUniversity of California San Francisco, Cellular Molecular Pharmacology, San Francisco, CA, USA.ORCID 0000-0002-0726-141X
Bertrand RaynalDépartement de Biologie structurale et chimie, Plateforme de biophysique moléculaire, Institut Pasteur, Paris, France.ORCID 0000-0001-5634-0408
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1GA, UK.ORCID 0000-0003-1144-9877
Hilde De ReuseDépartement de Microbiologie, Unité Pathogenèse de Helicobacter, UMR CNRS 6047, Institut Pasteur, Paris, France. hdereuse@pasteur.fr.ORCID 0000-0002-0100-4826
Centre National de la Recherche Scientifique · FRUniversity of Cambridge · GBInstitut Pasteur · FRUniversity of California, San Francisco · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

In the gastric pathogen Helicobacter pylori, post-transcriptional regulation relies strongly on the activity of the essential ribonuclease RNase J. Here, we elucidated the crystal and cryo-EM structures of RNase J and determined that it assembles into dimers and tetramers in vitro. We found that RNase J extracted from H. pylori is acetylated on multiple lysine residues. Alanine substitution of several of these residues impacts on H. pylori morphology, and thus on RNase J function in vivo. Mutations of Lysine 649 modulates RNase J oligomerization in vitro, which in turn influences ribonuclease activity in vitro. Our structural analyses of RNase J reveal loops that gate access to the active site and rationalizes how acetylation state of K649 can influence activity. We propose acetylation as a regulatory level controlling the activity of RNase J and its potential cooperation with other enzymes of RNA metabolism in H. pylori.

Indexed as

Helicobacter pyloriRibonucleasesAcetylationEndoribonucleasesLysineRibonuclease, PancreaticEndoribonucleasesLysineRibonuclease, PancreaticRibonucleases

Identifiers

PMID38057323
PMCPMC10700544
OpenAlexW4389389602

What OpenQuestion holds

Textmetadata
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.