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

dc.rights.licenseopenen_US
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMARTINEZ, Denis
dc.contributor.authorMORVAN, Estelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
hal.structure.identifierInstitut Polytechnique de Bordeaux
dc.contributor.authorGRELARD, Axelle
dc.contributor.authorKAUFFMANN, Brice
dc.contributor.authorWAEYTENS, Jehan
dc.contributor.authorWIEN, Frank
dc.contributor.authorARLUISON, Veronique
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.date.accessioned2024-04-18T07:57:18Z
dc.date.available2024-04-18T07:57:18Z
dc.date.issued2023-12
dc.identifier.issn2399-3642en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199214
dc.description.abstractEnAbstract 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.
dc.language.isoENen_US
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.title.enHfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s42003-023-05462-1en_US
dc.subject.halChimieen_US
bordeaux.journalCommunications Biologyen_US
bordeaux.page1075en_US
bordeaux.volume6en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue1en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-04284610
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Communications%20Biology&rft.date=2023-12&rft.volume=6&rft.issue=1&rft.spage=1075&rft.epage=1075&rft.eissn=2399-3642&rft.issn=2399-3642&rft.au=BERBON,%20Melanie&MARTINEZ,%20Denis&MORVAN,%20Estelle&GRELARD,%20Axelle&KAUFFMANN,%20Brice&rft.genre=article


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