Concerted action of plasmid maintenance functions: partition complexes create a requirement for dimer resolution

Mol Microbiol. 2006 Dec;62(5):1447-59. doi: 10.1111/j.1365-2958.2006.05454.x. Epub 2006 Oct 24.


Partition of prokaryotic DNA requires formation of specific protein-centromere complexes, but an excess of the protein can disrupt segregation. The mechanisms underlying this destabilization are unknown. We have found that destabilization by the F plasmid partition protein, SopB, of plasmids carrying the F centromere, sopC, results from the capacity of the SopB-sopC partition complex to stimulate plasmid multimerization. Mutant SopBs unable to destabilize failed to increase multimerization. Stability of wild-type mini-F, whose ResD/rfsF site-specific recombination system enables it to resolve multimers to monomers, was barely affected by excess SopB. Destabilization of plasmids lacking the rfsF site was suppressed by recF, recO and recR, but not by recB, mutant alleles, indicating that multimerization is initiated from single-strand gaps. SopB did not alter the amounts or distribution of replication intermediates, implying that SopB-DNA complexes do not create single-strand gaps by blocking replication forks. Rather, the results are consistent with SopB-DNA complexes channelling gapped molecules into the RecFOR recombination pathway. We suggest that extended SopB-DNA complexes increase the likelihood of recombination between sibling plasmids by keeping them in close contact prior to SopA-mediated segregation. These results cast plasmid site-specific resolution in a new role - compensation for untoward consequences of partition complex formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Chromosome Segregation*
  • Dimerization
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / metabolism
  • Plasmids / genetics
  • Plasmids / physiology*
  • Protein Conformation


  • Bacterial Proteins
  • Escherichia coli Proteins
  • SopB protein, Bacteria
  • SopB protein, E coli
  • SopA protein, Bacteria