A novel toxin-antitoxin operon talA/B from the Gram-positive bacterium Leifsonia xyli subsp. cynodontis.

ABSTRACT

Here we report a toxin-antitoxin (TA) operon talAB identified from the Gram-positive bacterium Leifsonia xyli subsp. cynodontis. It is shown that talB encodes a broad-host cytotoxin functioning in different Gram-positive bacteria, while talA encodes its antidote. TalA and TalB form different hetero-oligomers in vitro; these hetero-oligomers, but not the antitoxin TalA, strongly bind to the talAB promoter region containing two inverted repeats. This represents a new mechanism of binding the promoter of a TA operon by the toxin and antitoxin complexes.