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Background  Bacterial DNA replication restart pathways facilitate reinitiation of DNA replication following disruptive encounters of a replisome with DNA damage, thereby allowing complete and faithful duplication of the genome. In  Neisseria gonorrhoeae , the primosome proteins that catalyze DNA replication restart differ from the well-studied primosome proteins of  E. coli  with respect to the number of proteins involved and the affinities of their physical interactions: the PriA:PriB interaction is weak in  E. coli , but strong in  N. gonorrhoeae , and the PriB:DNA interaction is strong in  E. coli , but weak in  N. gonorrhoeae . In this study, we investigated the functional consequences of this affinity reversal.    Results  We report that  N. gonorrhoeae  PriA's DNA binding and unwinding activities are similar to those of  E. coli  PriA, and  N. gonorrhoeae  PriA's helicase activity is stimulated by its cognate PriB, as it is in  E. coli . This finding is significant because  N. gonorrhoeae  PriB's single-stranded DNA binding activity is weak relative to that of  E. coli  PriB, and in  E. coli , PriB's single-stranded DNA binding activity is important for PriB stimulation of PriA helicase. Furthermore, a  N. gonorrhoeae  PriB variant defective for binding single-stranded DNA can stimulate PriA's helicase activity, suggesting that DNA binding by PriB might not be important for PriB stimulation of PriA helicase in  N. gonorrhoeae . We also demonstrate that  N. gonorrhoeae  PriB stimulates ATP hydrolysis catalyzed by its cognate PriA. This activity of PriB has not been observed in  E. coli , and could be important for PriB stimulation of PriA helicase in  N. gonorrhoeae .    Conclusions  The results of this study demonstrate that a bacterial PriB homolog with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase. While it remains unclear if  N. gonorrhoeae  PriB's weak DNA binding activity is required for PriB stimulation of PriA helicase, the ability of PriB to stimulate PriA-catalyzed ATP hydrolysis could play an important role. Thus, the weak interaction between  N. gonorrhoeae  PriB and DNA might be compensated for by the strong interaction between PriB and PriA, which could result in allosteric activation of PriA's ATPase activity.

A bacterial PriB with weak single-stranded DNA binding activity can stimulate the DNA unwinding activity of its cognate PriA helicase