Protein Domain : RelB antitoxin/Antitoxin DinJ IPR007337

Type  Family
Description  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. Several toxin/antitoxin pairs may occur in a single species. RelE and RelB form a toxin-antitoxin system; RelE cleaves mRNA during translation on the ribosome [ , , ]. RelB binds and inhibits RelE and it regulates transcription by operator binding and conditional cooperativity controlled by RelE. RelE and RelB form a V-shaped heterotetrameric complex which has a ribbon-helix-helix (RHH) dimerization domain at the apex. [].DinJ is an antitoxin component of a toxin-antitoxin (TA) module. It is a labile antitoxin that counteracts the effect of the YafQ toxin [ ]. It forms a heterotetrameric complex with YafQ and the structure of this complex revealed that the N-terminal region of DinJ folds into a ribbon-helix-helix motif that dimerises for DNA recognition, and the C-terminal portion of each DinJ wraps around a YafQ molecule []. Together, they they bind their own promoter, and by analogy to other TA modules probably repress its expression. Cell death governed by the mazEF and dinJ-yafQ TA modules seems to play a role in biofilm formation [, , ].
Short Name  RelB/DinJ

1 Child Features

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