Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure - Archive ouverte HAL Access content directly
Journal Articles Communications Biology Year : 2023

Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure

Abstract

Abstract Hfq is a pleitropic actor that serves as stress response and virulence factor in the bacterial cell. To execute its multiple functions, Hfq assembles into symmetric torus-shaped hexamers. Extending outward from the hexameric core, Hfq presents a C-terminal region, described as intrinsically disordered in solution. Many aspects of the role and the structure of this region remain unclear. For instance, in its truncated form it can promote amyloid-like filament assembly. Here, we show that a minimal 11-residue motif at the C-terminal end of Hfq assembles into filaments with amyloid characteristics. Our data suggest that the full-length Hfq in its filamentous state contains a similar molecular fingerprint than that of the short β-strand peptide, and that the Sm-core structure is not affected by filament formation. Hfq proteins might thus co-exist in two forms in vivo, either as isolated, soluble hexamers or as self-assembled hexamers through amyloid-reminiscent interactions, modulating Hfq cellular functions.
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hal-04284610 , version 1 (14-11-2023)

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Mélanie Berbon, Denis Martinez, Estelle Morvan, Axelle Grélard, Brice Kauffmann, et al.. Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure. Communications Biology, 2023, 6 (1), pp.1075. ⟨10.1038/s42003-023-05462-1⟩. ⟨hal-04284610⟩
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