Abstract

FtsZ, a core and widely conserved cell division protein that orchestrates the septum formation at the midcell and recruits at least 10 downstream cell division proteins in the architecture of divisome scaffold. The intracellular environment of bacteria with ~1 mM GTP nucleotide pool enables monomeric FtsZ subunits to process the self-association and assembly into Z-ring which functions as a cytokinetic contractile ring for division machinery.1 FtsZ polymerization can be either longitudinal or lateral, or both, depending on the intrinsic property of proteins. The longitudinal association of FtsZ is driven by its GTP binding affinity and hydrolysis rate upon subunit-subunit association, while the lateral association of FtsZ depends on the charge state of its C-terminal variable region.2 To date, it is reported that Staphylococcus aureus FtsZ (SaFtsZ) has a weak GTPase activity causing slow polymerization and depolymerization, and a relatively higher critical concentration for protein assembly compared to other strains. This poster will focus on the in vitro study of SaFtsZ, and present the stability of protein secondary structure, optimal buffer condition for the polymerization of SaFtsZ alone, quantitative analysis of SaFtsZ monomer/polymer fractions induced by guanosine nucleotides, as well as the transmission electron micrographs of negatively stained SaFtsZ polymers in higher-order structure. 

References:

1. S. Huecas, A. J. Canosa-Valls, L. Araújo-Bazán, F. M. Ruiz, D. V. Laurents, C. Fernández-Tornero and J. M. Andreu, The FEBS Journal, 2020, 287, 4048-4067.
2. N. Silber, C. L. M. d. Opitz, C. Mayer and P. Sass, Future Microbiology, 2020, 15, 801-831.