Structural insights into chaperone addiction of toxin-antitoxin systems

Valérie Guillet, Patricia Bordes, Cécile Bon, Julien Marcoux, Virginie Gervais, Ambre Julie Sala, Suzana Dos Reis, Nawel Slama, Israel Mares-Mejía, Anne-Marie Cirinesi, Laurent Maveyraud, Pierre Genevaux () and Lionel Mourey ()
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Valérie Guillet: IPBS, Université de Toulouse, CNRS, UPS
Patricia Bordes: Université de Toulouse, CNRS, UPS
Cécile Bon: IPBS, Université de Toulouse, CNRS, UPS
Julien Marcoux: IPBS, Université de Toulouse, CNRS, UPS
Virginie Gervais: IPBS, Université de Toulouse, CNRS, UPS
Ambre Julie Sala: Université de Toulouse, CNRS, UPS
Suzana Dos Reis: IPBS, Université de Toulouse, CNRS, UPS
Nawel Slama: Université de Toulouse, CNRS, UPS
Israel Mares-Mejía: IPBS, Université de Toulouse, CNRS, UPS
Anne-Marie Cirinesi: Université de Toulouse, CNRS, UPS
Laurent Maveyraud: IPBS, Université de Toulouse, CNRS, UPS
Pierre Genevaux: Université de Toulouse, CNRS, UPS
Lionel Mourey: IPBS, Université de Toulouse, CNRS, UPS

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-08747-4

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