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Molecular anatomy of the Streptococcus pyogenes pSM19035 partition and segrosome complexes.


ABSTRACT: Vancomycin or erythromycin resistance and the stability determinants, ?? and ???, of Enterococci and Streptococci plasmids are genetically linked. To unravel the mechanisms that promoted the stable persistence of resistance determinants, the early stages of Streptococcus pyogenes pSM19035 partitioning were biochemically dissected. First, the homodimeric centromere-binding protein, ?2, bound parS DNA to form a short-lived partition complex 1 (PC1). The interaction of PC1 with homodimeric ? [?2 even in the apo form (Apo-?2)], significantly stimulated the formation of a long-lived ?2·parS complex (PC2) without spreading into neighbouring DNA sequences. In the ATP·Mg2+ bound form, ?2 bound DNA, without sequence specificity, to form a transient dynamic complex (DC). Second, parS bound ?2 interacted with and promoted ?2 redistribution to co-localize with the PC2, leading to transient segrosome complex (SC, parS·?2·?2) formation. Third, ?2, in the SC, interacted with a second SC and promoted formation of a bridging complex (BC). Finally, increasing ?2 concentrations stimulated the ATPase activity of ?2 and the BC was disassembled. We propose that PC, DC, SC and BC formation were dynamic processes and that the molar ?2:?2 ratio and parS DNA control their temporal and spatial assembly during partition of pSM19035 before cell division.

SUBMITTER: Soberon NE 

PROVIDER: S-EPMC3074150 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

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Molecular anatomy of the Streptococcus pyogenes pSM19035 partition and segrosome complexes.

Soberón Nora E NE   Lioy Virginia S VS   Pratto Florencia F   Volante Andrea A   Alonso Juan C JC  

Nucleic acids research 20101207 7


Vancomycin or erythromycin resistance and the stability determinants, δω and ωεζ, of Enterococci and Streptococci plasmids are genetically linked. To unravel the mechanisms that promoted the stable persistence of resistance determinants, the early stages of Streptococcus pyogenes pSM19035 partitioning were biochemically dissected. First, the homodimeric centromere-binding protein, ω2, bound parS DNA to form a short-lived partition complex 1 (PC1). The interaction of PC1 with homodimeric δ [δ2 ev  ...[more]

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