The SXT conjugative element and linear prophage N15 encode toxin-antitoxin-stabilizing systems homologous to the tad-ata module of the Paracoccus aminophilus plasmid pAMI2.


:A group of proteic toxin-antitoxin (TA) cassettes whose representatives are widely distributed among bacterial genomes has been identified. These cassettes occur in chromosomes, plasmids, bacteriophages, and noncomposite transposons, as well as in the SXT conjugative element of Vibrio cholerae. The following four homologous loci were subjected to detailed comparative studies: (i) tad-ata from plasmid pAMI2 of Paracoccus aminophilus (the prototype of this group), (ii) gp49-gp48 from the linear bacteriophage N15 of Escherichia coli, (iii) s045-s044 from SXT, and (iv) Z3230-Z3231 from the genomic island of enterohemorrhagic Escherichia coli O157:H7 strain EDL933. Functional analysis revealed that all but one of these loci (Z3230-Z3231) are able to stabilize heterologous replicons, although the host ranges varied. The TA cassettes analyzed have the following common features: (i) the toxins are encoded by the first gene of each operon; (ii) the antitoxins contain a predicted helix-turn-helix motif of the XRE family; and (iii) the cassettes have two promoters that are different strengths, one which is located upstream of the toxin gene and one which is located upstream of the antitoxin gene. All four toxins tested are functional in E. coli; overexpression of the toxins (in the absence of antitoxin) results in a bacteriostatic effect manifested by elongation of bacterial cells and growth arrest. The toxins have various effects on cell viability, which suggests that they may recognize different intracellular targets. Preliminary data suggest that different cellular proteases are involved in degradation of antitoxins encoded by the loci analyzed.


J Bacteriol


Journal of bacteriology


Dziewit L,Jazurek M,Drewniak L,Baj J,Bartosik D




Has Abstract


2007-03-01 00:00:00














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    authors: Sutcliffe J,Blumenthal R,Walter A,Foulds J

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  • Structure and function of cold shock proteins in archaea.

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    authors: Giaquinto L,Curmi PM,Siddiqui KS,Poljak A,DeLong E,DasSarma S,Cavicchioli R

    更新日期:2007-08-01 00:00:00

  • Use of hupS::lacZ gene fusion to study regulation of hydrogenase expression in Rhodobacter capsulatus: stimulation by H2.

    abstract::The Escherichia coli beta-galactosidase enzyme was used as a reporter molecule for genetic fusions in Rhodobacter capsulatus. DNA fragments that were from the upstream region of the hydrogenase structural operon hupSLM and contained 5' hupS sequences were fused in frame to a promoterless lacZ gene, yielding fusion pro...

    journal_title:Journal of bacteriology

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    authors: Colbeau A,Vignais PM

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    authors: Yan LP,Hitchins AD

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  • The recombinase IntA is required for excision of esp-containing ICEEfm1 in Enterococcus faecium.

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    journal_title:Journal of bacteriology

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    authors: Taschner PE,Verest JG,Woldringh CL

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  • Comparative aspects of some bacterial dehydrogenases and transhydrogenases.

    abstract::Ragland, T. E. (Brandeis University, Waltham, Mass.), T. Kawasaki, and J. M. Lowenstein. Comparative aspects of some bacterial dehydrogenases and transhydrogenases. J. Bacteriol. 91:236-244. 1966.-Twenty-eight diverse bacterial species were surveyed for the activities and coenzyme specificities of four enzymes: isocit...

    journal_title:Journal of bacteriology

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    authors: Ragland TE,Kawasaki T,Lowenstein JM

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