Structural insights into chaperone addiction of toxin-antitoxin systems - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2019

Structural insights into chaperone addiction of toxin-antitoxin systems

Résumé

SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain SecB homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response to stress. In such TA-chaperone (TAC) systems, SecB assists the folding and prevents degradation of the antitoxin, thus facilitating toxin inhibition. Chaperone dependency is conferred by a C-terminal extension in the antitoxin known as chaperone addiction (ChAD) sequence, which makes the antitoxin aggregation-prone and prevents toxin inhibition. Using TAC of Mycobacterium tuberculosis, we present the structure of a SecB-like chaperone bound to its ChAD peptide. We find differences in the binding interfaces when compared to SecB–SecA or SecB-preprotein complexes, and show that the antitoxin can reach a functional form while bound to the chaperone. This work reveals how chaperones can use discrete surface binding regions to accommodate different clients or partners and thereby expand their substrate repertoire and functions.
Fichier principal
Vignette du fichier
nature_communications_2019_10_782.pdf (3.23 Mo) Télécharger le fichier
publisher_correction.pdf (311.84 Ko) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-02335509 , version 1 (21-10-2020)

Identifiants

Citer

Valerie Guillet, Patricia Bordes, Cécile Bon, Julien Marcoux, Virginie Gervais, et al.. Structural insights into chaperone addiction of toxin-antitoxin systems. Nature Communications, 2019, 10 (1), ⟨10.1038/s41467-019-08747-4⟩. ⟨hal-02335509⟩
108 Consultations
58 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More