PXD027670

PXD027670 is an original dataset announced via ProteomeXchange.

Title	Acetylation regulates the oligomerization state and activity of RNase J, the major ribonuclease of Helicobacter pylori
Description	In Helicobacter pylori, the major actor in post-transcriptional regulation is an RNA degradosome assembly composed of the essential ribonuclease RNase J and the DEAD-box RNA helicase RhpA. Here, we describe the oligomeric state and post-translational modifications of this protein complex. Our crystal structure of RNase J at 2.75 Å resolution reveals a homotetrameric quaternary state, and solution studies show that purified RNase J forms monomers and dimers, that RhpA is a monomer, and that the two proteins interact to form a stable complex with a 1:1 stoichiometry. Using mass spectrometry, we observed that RNase J is acetylated on multiple residues, one of which, K649, is important for RNase J oligomerization. Mutations targeting this residue and others affect the dimerization and in vitro activity of RNase J, suggesting that the dimer is the active form. In H. pylori, we observed that several of the identified acetylated residues impact on cell morphology, suggesting their importance for RNase J cellular function. Using H. pylori mutants, we found that several pathways contribute to RNase J acetylation. We propose acetylation as a regulatory level controlling RNase J properties and as a consequence the activity of the H. pylori RNA degradosome.
HostingRepository	PRIDE
AnnounceDate	2023-12-12
AnnouncementXML	Submission_2023-12-12_08:21:28.993.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Thibaut Douché
SpeciesList	scientific name: Helicobacter pylori B8; NCBI TaxID: 693745;
ModificationList	L-methionine (S)-sulfoxide; mono N-acetylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2021-07-30 04:45:40	ID requested
⏵ 1	2023-12-12 08:21:29	announced

10.1038/S41467-023-43825-8;

submitter keyword: proteomics,Helicobacter pylori, Q Exactive Plus, K-acetylation

Hilde De Reuse
contact affiliation	Unité de Pathogenèse de Helicobacter, CNRS UMR 2001, Département de Microbiologie, Institut Pasteur, Paris, France
contact email	hilde.de-reuse@pasteur.fr
lab head
Thibaut Douché
contact affiliation	Institut Pasteur
contact email	thibaut.douche@pasteur.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD027670
     1. Label: PRIDE project
     2. Name: Acetylation regulates the oligomerization state and activity of RNase J, the major ribonuclease of Helicobacter pylori