REPLICATION-SPECIFIC CONVERSION OF THE STAPHYLOCOCCUS-AUREUS PT181 INITIATOR PROTEIN FROM AN ACTIVE HOMODIMER TO AN INACTIVE HETERODIMER

The Staphylococcus aureus rolling circle plasmid pT181 regulates its replication by controlling the synthesis of its initiator protein RepC. RepC is inactivated during pT181 replication by the addition of an oligodeoxynucleotide, giving rise to a new form, RepC(*). We analyzed RepC and RepC(*) in four classes of mutants: plasmid copy number mutants, two classes of RepC mutants affecting different portions of the protein and oriC (origin) mutants. We have found that in the cell with wild-type RepC there are similar relative amounts of RepC and RepC(*), regardless of copy number, and that the conversion of RepC to RepC(*) is replication dependent. Genetic and biochemical evidence is presented that RepC functions as a dimer and that during replication the RepC homodimer is converted to the RepC/RepC(*) heterodimer.