Skip to Main content Skip to Navigation
Journal articles

Membrane association of the bacterial riboregulator Hfq and functional perspectives.

Abstract : Hfq is a bacterial RNA binding protein that carries out several roles in genetic expression regulation, mainly at the post-transcriptional level. Previous studies have shown its importance in growth and virulence of bacteria. Here, we provide the direct observation of its ability to interact with membranes. This was established by co-sedimentation assay, cryo-transmission electron (cryo-TEM) and atomic force (AFM) microscopies. Furthermore, our results suggest a role for its C-terminus amyloidogenic domain in membrane disruption. Precisely, AFM images of lipid bilayers in contact with Hfq C-terminus fibrils show the emergence of holes with a size dependent on the time of interaction. Cryo-TEM observations also show that liposomes are in contact with clusters of fibrils, with occasional deformation of the vesicles and afterward the apparition of a multitude of tiny vesicles in the proximity of the fibrils, suggesting peptide-induced breakage of the liposomes. Finally, circular dichroism spectroscopy demonstrated a change in the secondary structure of Hfq C-terminus upon interaction with liposomes. Altogether, these results show an unexpected property of Hfq and suggest a possible new role for the protein, exporting sRNA outside of the bacterial cell.
Complete list of metadata

Cited literature [60 references]  Display  Hide  Download
Contributor : Antoine Malabirade Connect in order to contact the contributor
Submitted on : Thursday, September 21, 2017 - 1:49:02 PM
Last modification on : Saturday, June 25, 2022 - 10:26:33 PM


2017 - Membrane association of...
Publication funded by an institution


Distributed under a Creative Commons Attribution 4.0 International License



Antoine Malabirade, Javier Morgado-Brajones, Sylvain Trépout, Frank Wien, Ileana Marquez, et al.. Membrane association of the bacterial riboregulator Hfq and functional perspectives.. Scientific Reports, Nature Publishing Group, 2017, 7, pp.10724. ⟨10.1038/s41598-017-11157-5⟩. ⟨cea-01591449⟩



Record views


Files downloads