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Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation

dc.rights.licenseopenen_US
dc.contributor.authorCAMARA-ALMIRON, Jesus
dc.contributor.authorDOMINGUEZ-GARCIA, Laura
dc.contributor.authorEL MAMMERI, Nadia
dc.contributor.authorLENDS, Alons
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorDE VICENTE, Antonio
hal.structure.identifierInstitut Européen de Chimie et Biologie [IECB]
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorROMERO, Diego
dc.date.accessioned2024-04-19T07:01:47Z
dc.date.available2024-04-19T07:01:47Z
dc.date.issued2023-09-22
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/199232
dc.description.abstractEnAbstract Biofilms are bacterial communities that result from a cell differentiation process leading to the secretion of an extracellular matrix (ECM) by part of the population. In Bacillus subtilis , the main protein component of the ECM is TasA, which forms a fiber-based scaffold that confers structure to the ECM. The N-terminal half of TasA is strongly conserved among Bacillus species and contains a protein domain, the rigid core (RcTasA), which is critical for the structural and functional properties of the recombinant protein. In this study, we demonstrate that recombinantly purified RcTasA in vitro retains biochemical properties previously observed for the entire protein. Further analysis of the RcTasA amino acid sequence revealed two aggregation-prone stretches and a region of imperfect amino acid repeats, which are known to contribute to functional amyloid assembly. Biochemical characterization of these stretches found in RcTasA revealed their amyloid-like capacity in vitro, contributing to the amyloid nature of RcTasA. Moreover, the study of the imperfect amino acid repeats revealed the critical role of residues D64, K68 and D69 in the structural function of TasA. Experiments with versions of TasA carrying the substitutions D64A and K68AD69A demonstrated a partial loss of function of the protein either in the assembly of the ECM or in the stability of the core and amyloid-like properties. Taken together, our findings allow us to better understand the polymerization process of TasA during biofilm formation and provide knowledge into the sequence determinants that promote the molecular behavior of protein filaments in bacteria.
dc.language.isoENen_US
dc.title.enMolecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s41522-023-00437-wen_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]en_US
bordeaux.journalnpj Biofilms and Microbiomesen_US
bordeaux.page68en_US
bordeaux.volume9en_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-04307919
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=npj%20Biofilms%20and%20Microbiomes&rft.date=2023-09-22&rft.volume=9&rft.issue=1&rft.spage=68&rft.epage=68&rft.au=CAMARA-ALMIRON,%20Jesus&DOMINGUEZ-GARCIA,%20Laura&EL%20MAMMERI,%20Nadia&LENDS,%20Alons&HABENSTEIN,%20Birgit&rft.genre=article


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