Abstract

Toxin–antitoxin (TA) modules regulate metabolism and viability of bacteria and archaea. In type II TA systems these functions are generally thought to be performed by two small proteins. However, evidence is increasing that the toxins are much more diverse and can form multi-domain proteins. Recently, we published a novel type II TA system in which toxin and antitoxin are covalently linked into a single polypeptide chain. In this review we summarize the current knowledge on these elongated toxin homologs and provide perspectives for future study.

Highlights

  • Bacterial type II toxin–antitoxin (TA) systems were already identified in 1983 as bicistronic operons that ensure stable plasmid maintenance in bacteria (Ogura and Hiraga 1983)

  • In addition to the here exemplified type II TA systems, similar functions have been ascribed for a number of other type II TA systems as well, and even overlapping functions have been proposed for some systems (De la Cruz et al 2013; Magnuson 2007; Van Melderen and Saavedra De Bast 2009; Wang and Wood 2011)

  • Bioinformatic analyses browsing the increasing number of available microbial genomes revealed that type II TA systems are widespread in both bacteria and archaea where they can exist in multiple copies on plasmids as well as on chromosomes (Leplae et al 2011; Makarova et al 2009; Sberro et al 2013; Sevin and Barloy-Hubler 2007; Shao et al 2011)

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Summary

Introduction

Bacterial type II toxin–antitoxin (TA) systems were already identified in 1983 as bicistronic operons that ensure stable plasmid maintenance in bacteria (Ogura and Hiraga 1983). Type II TA systems are highly prevalent on the chromosome of bacteria and additional functions apart from being simple selfish entities that secure stable maintenance of mobile genetic elements are reported (Van Melderen and Saavedra De Bast 2009).

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