REGULAR ARTICLES Cell Research (2004); 14(3): 208-216 Characterization of a novel toxin-antitoxin module, VapBC, encoded by Leptospira interrogans chromosome Yi Xuan ZHANG1, 2, Xiao Kui GUO3, Chuan WU2, Bo BI1, Shuang Xi REN4, Chun Fu WU1, Guo Ping ZHAO2, 4 1Pharmaceutical Department, Shenyang
Pharmaceutical University, 103 Wenhua Road, Shenhe District, Shenyang
110016,China. Received, Oct 21, 2003 Revised, Apr 25, 2004 Accepted, Apr 28, 2004
Comparative genomic analysis of the coding sequences (CDSs) of Leptospira interrogans revealed a pair of closely linked genes homologous to the vapBC loci of many other bacteria with respect to both deduced amino acid sequences and operon organizations. Expression of single vapC gene in Escherichia coli resulted in inhibition of bacterial growth, whereas co-expression of vapBC restored the growth effectively. This phenotype is typical for three other characterized toxin-antitoxin systems of bacteria, i.e., mazEF[1], relBE[2] and chpIK[3]. The VapC proteins of bacteria and a thermophilic archeae, Solfolobus tokodaii, form a structurally distinguished group of toxin different from the other known toxins of bacteria. Phylogenetic analysis of both toxins and antitoxins of all categories indicated that although toxins were evolved from divergent sources and may or may not follow their speciation paths (as indicated by their 16s RNA sequences), co-evolution with their antitoxins was obvious. Keywords: Leptospria, toxin-antitoxin system, VapBC, co-evolution, speciation.
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