Titre
Molecular characterization of the N-terminal half of TasA during amyloid-like assembly and its contribution to Bacillus subtilis biofilm formation.
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Cámara-Almirón, J.
Auteure/Auteur
Domínguez-García, L.
Auteure/Auteur
El Mammeri, N.
Auteure/Auteur
Lends, A.
Auteure/Auteur
Habenstein, B.
Auteure/Auteur
de Vicente, A.
Auteure/Auteur
Loquet, A.
Auteure/Auteur
Romero, D.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
2055-5008
Statut éditorial
Publié
Date de publication
2023-09-22
Volume
9
Numéro
1
Première page
68
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Publication Status: epublish
Résumé
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.
PID Serval
serval:BIB_D391CA0BBB25
PMID
Open Access
Oui
Date de création
2023-09-29T13:23:29.969Z
Date de création dans IRIS
2025-05-21T01:03:36Z
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Nom
37739955_BIB_D391CA0BBB25.pdf
Version du manuscrit
published
Licence
https://creativecommons.org/licenses/by/4.0
Taille
6.29 MB
Format
Adobe PDF
PID Serval
serval:BIB_D391CA0BBB25.P001
URN
urn:nbn:ch:serval-BIB_D391CA0BBB259
Somme de contrôle
(MD5):02b3b3f760c1203736093efd8e54f244