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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Guillet V,Bordes P,Bon C,Marcoux J,Gervais V,Sala AJ,Dos Reis S,Slama N,Mares-Mejía I,Cirinesi AM,Maveyraud L,Genevaux P,Mourey Ldoi
10.1038/s41467-019-08747-4subject
Has Abstractpub_date
2019-02-15 00:00:00pages
782issue
1issn
2041-1723pii
10.1038/s41467-019-08747-4journal_volume
10pub_type
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