Understanding FtsZ assembly: cues from the behavior of its N- and C-terminal domains

FtsZ polymerizes to form a cytokinetic ring at the center of a bacterial cell, which engineers bacterial cell division. FtsZ consists of N-terminal and C-terminal core domains followed by a C-terminal spacer and a conserved C-terminal tail region. Though it has been reported that both N- and C-domains can fold independently, the assembly behaviors of the N- and C-domains are not clear. In this study, we created five truncated constructs of Bacillus subtilis FtsZ, two N-domain and three C-domain constructs, and expressed and purified them. We determined their assembly properties and their effect on the assembly of full-length FtsZ to gain insight into the mechanism of FtsZ polymerization. We found that the N-domain of B. subtilis FtsZ can polymerize on its own in a GTP-dependent manner. Further, we obtained evidence indicating that the N-domain could bind to GTP but could not hydrolyze GTP by itself. In addition, the N-domain was found to inhibit the assembly of full-length FtsZ. Interestingly, the N-domain was found to enhance the GTPase activity of full-length FtsZ. An analysis of the effects of the N- and C-domains on FtsZ assembly indicated that the assembly of FtsZ might be directional. The work has provided new insight into the assembly characteristics of FtsZ domains and the mechanism of FtsZ polymerization.