Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq.
Hfq
bacterial amyloid
lipid–protein interaction
membrane insertion
protein self-assembly
regulatory RNA
small non-coding RNA
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
05 Aug 2022
05 Aug 2022
Historique:
received:
28
06
2022
revised:
01
08
2022
accepted:
02
08
2022
entrez:
12
8
2022
pubmed:
13
8
2022
medline:
16
8
2022
Statut:
epublish
Résumé
Hfq is a pleiotropic regulator that mediates several aspects of bacterial RNA metabolism. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, usually via its interaction with small regulatory RNAs. Previously, we showed that the Hfq C-terminal region forms an amyloid-like structure and that these fibrils interact with membranes. The immediate consequence of this interaction is a disruption of the membrane, but the effect on Hfq structure was unknown. To investigate details of the mechanism of interaction, the present work uses different in vitro biophysical approaches. We show that the Hfq C-terminal region influences membrane integrity and, conversely, that the membrane specifically affects the amyloid assembly. The reported effect of this bacterial master regulator on membrane integrity is discussed in light of the possible consequence on small regulatory RNA-based regulation.
Identifiants
pubmed: 35955871
pii: ijms23158739
doi: 10.3390/ijms23158739
pmc: PMC9369112
pii:
doi:
Substances chimiques
Amyloidogenic Proteins
0
Bacterial Proteins
0
Escherichia coli Proteins
0
Host Factor 1 Protein
0
RNA, Bacterial
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Centre National de la Recherche Scientifique
ID : IEA/PICS 08254
Organisme : ANR
ID : ANR-11-IDEX-0003-02
Organisme : CNRS
ID : Momentum
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