The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionarily distinct subgroup of the ParA superfamily

作者：Hayes F^*

来源：Molecular Microbiology, 2000, 37(3): 528-541.

DOI：10.1046/j.1365-2958.2000.02030.x

The segregational stability of bacterial, low-copy-number plasmids is promoted primarily by active partition, The plasmid-specified components of the prototypical pi plasmid partition system consist of two proteins, ParA (44.3 kDa) and pars (38.5 kDa), which, in conjunction with integration host factor, form a nucleoprotein complex at the plasmid partition site, parS. This complex is the probable substrate for the directed temporal and spatial intracellular movement of plasmids before cell division. The genetic organization of the partition cassette of the multidrug resistance plasmid TP228 differs markedly from that of the pi paradigm. The TP228 system includes a novel member (ParF; 22.0 kDa) of the ParA superfamily of ATPases, of which the pi ParA protein is the archetype. However, the ParF protein and its immediate relatives form a discrete subgroup of the ParA superfamily, which evolutionarily is more related to the MinD subgroup of cell division proteins than to ParA of P1. The TP228 and P1 partition modules differ further in that the former does not include a parS homologue, but does specify a protein (ParG; 8.6 kDa) unrelated to pare. Homologues of the parF gene are widely disseminated on eubacterial genomes, suggesting that ParF-mediated partition may be a common mechanism by which plasmid segregational stability is achieved.

• 出版日期2000-8