Does the Hfq Protein Contribute to RNA Cargo Translocation into… – Weblog • by NanoWorld®


Gram-negative micro organism launch outer membrane vesicles (OMVs) that play a central function in host–pathogen interactions by transporting biomolecules, together with proteins and nucleic acids. On this article, Marisela Velez and Véronique Arluison examine the function of the RNA chaperone Hfq in mediating the interplay of small regulatory RNAs (sRNAs) with bacterial membranes.

On this article, it’s proven that RNA binding to the internal membrane of Escherichia coli happens in an Hfq-dependent method. The research additional demonstrates that membrane composition is a key issue on this course of, with cardiolipin-rich lipid domains considerably enhancing RNA–membrane interactions. These findings present new perception into the mechanism of RNA translocation from the cytoplasm to the periplasm, supporting its subsequent incorporation into OMVs.

Atomic power microscopy (AFM) was used to confirm the formation and integrity of supported lipid bilayers and to observe peptide–membrane interactions. Imaging was carried out in tapping mode utilizing a NanoWorld PNP-DB AFM probe with a resonance frequency of 15 kHz and a spring fixed of 0.48 N/m. Measurements have been carried out in liquid setting, enabling high-resolution characterization of biologically related membrane constructions.

This work highlights the significance of AFM-based evaluation for learning lipid–protein interactions and gives new understanding of RNA transport mechanisms in bacterial methods.

Determine 1
E. coli lipid bilayer incubated within the absence (A) or presence (B) of Hfq-CTR. Panel (A) reveals the E. coli lipids bilayer. The peak profile below the road proven on the higher picture signifies that the domains are 0.8 nm increased than the remainder of the membrane. The decrease panel reveals a three-dimensional illustration of a small area. Panel (B) reveals the E. coli lipid bilayer incubated within the presence of Hfq-CTR. The peptide accrued on high of among the domains, producing 1 nm excessive areas in a few of them, as proven on the peak profile. The arrows level the areas the place the change in top happens.

Full quotation:
Velez, M.; Arluison, V.
Does the Hfq Protein Contribute to RNA Cargo Translocation into Bacterial Outer Membrane Vesicles?
Pathogens 2025, 14(4), 399.

https://doi.org/10.3390/pathogens14040399

License: CC BY 4.0 (https://creativecommons.org/licenses/by/4.0/)

 

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