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type II toxin-antitoxin system RelB/DinJ family antitoxin
RelE and RelB form a toxin-antitoxin system. RelE represses translation, probably through binding ribosomes ([1], [2]). RelB stably binds RelE, presumably deactivating it. [1]. 11274135. Purification of the RelB and RelE proteins of Escherichia coli: RelE binds to RelB and to ribosomes. Galvani C, Terry J, Ishiguro EE;. J Bacteriol 2001;183:2700-2703. [2]. 12123459. Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Pedersen K, Christensen SK, Gerdes K;. Mol Microbiol 2002;45:501-510. (from Pfam)
type II toxin-antitoxin (TA) system RelB/DinJ family antitoxin similar to Escherichia coli RelB, the antitoxin component of the RelE-RelB TA module; binds and inhibits the effect of cognate toxin RelE and functions as an autorepressor of relBE operon transcription
Plasmids may be maintained stably in bacterial populations through the action of addiction modules, in which a toxin and antidote are encoded in a cassette on the plasmid. In any daughter cell that lacks the plasmid, the toxin persists and is lethal after the antidote protein is depleted. Toxin/antitoxin pairs are also found on main chromosomes, and likely represent selfish DNA. Sequences in the seed for this alignment all were found adjacent to toxin genes. The resulting model appears to describe a narrower set of proteins than Pfam model PF04221, although many in the scope of this model are not obviously paired with toxin proteins. Several toxin/antitoxin pairs may occur in a single species.
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