Plasmodium falciparum single-stranded DNA-binding protein (PfSSB) interacts with PfPrex helicase and modulates its activity.

Plasmodium falciparum (Pf) apicoplast is an essential organelle harbouring a ~35-kb circular genome. Prokaryotic nature of this organelle and its components makes it an attractive therapeutic target. The single-stranded DNA-binding protein (SSB) and multidomain protein PfPrex are important apicoplast replication proteins. However, regulation of these proteins through protein-protein interaction remains largely unknown. Here, we report that P. falciparum single-stranded DNA-binding protein (PfSSB) interacts with PfPrex helicase and modulates its activity. N-terminal domain of PfSSB is involved in this interaction, whereas C-terminal domain plays a pivotal role in the modulation of helicase activity. These results further, to our knowledge, understand apicoplast DNA replication.