DNA replication and cell division complexes remain physically associated throughout the cell cycle in Helicobacter pylori.

The occurrence of drug-resistant strains exacerbates the difficulty of treating stomach cancer caused by Helicobacter pylori. DNA replication and cell division offer attractive targets for the development of antibacterial therapies. Both DNA replication and cell division in H. pylori start at one of the poles and terminate at the middle of the cell. The absence of a SlmA homolog and the presence of a unique Min CDE system may explain polar divisome assembly in Helicobacter. We previously observed the co-localization of replisome and divisome proteins; however, it is unclear if they interact directly. We report, for the first time, the interaction between two complexes in vitro and in vivo. These results highlight the mechanistic aspects of the unique polar co-assembly of the replisome/divisome complex in Helicobacter, through interactions among members of each component, which might be useful for identifying new targets.