Unraveling Membrane Perturbations Caused by the Bacterial Riboregulator Hfq

• Published in: International journal of molecular sciences Vol. 23; no. 15; p. 8739
• Main Authors: Turbant, Florian, Waeytens, Jehan, Campidelli, Camille, Bombled, Marianne, Martinez, Denis, Grélard, Axelle, Habenstein, Birgit, Raussens, Vincent, Velez, Marisela, Wien, Frank, Arluison, Véronique
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 05-08-2022; MDPI
• Subjects: Amyloid; Bacteria; bacterial amyloid; Binding sites; Cell division; Chemical Sciences; E coli; Fibrils; Gene expression; Gram-negative bacteria; Hfq; Lipids; Material chemistry; membrane insertion; Membranes; Metabolism; Peptides; protein self-assembly; Protein turnover; Proteins; regulatory RNA; small non-coding RNA; Spectrum analysis; Transmission electron microscopy; Hfq; Protein self-assembly; Bacterial amyloid; Lipid–protein interaction; Membrane insertion; Small non-coding RNA; Regulatory RNA
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms23158739

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.