Abstract
FtsZ is an essential and central protein for cell division in most bacteria. Because of its ability to organize into dynamic polymers at the cell membrane and recruit other protein partners to form a “divisome”, FtsZ is a leading target in the quest for new antibacterial compounds. Strategies to potentially arrest the essential and tightly regulated cell division process include perturbing FtsZ’s ability to interact with itself and other divisome proteins. Here, we discuss the available methodologies to screen for and characterize those interactions. In addition to assays that measure protein-ligand interactions in solution, we also discuss the use of minimal membrane systems and cell-like compartments to better approximate the native bacterial cell environment and hence provide a more accurate assessment of a candidate compound’s potential in vivo effect. We particularly focus on ways to measure and inhibit under-explored interactions between FtsZ and partner proteins. Finally, we discuss recent evidence that FtsZ forms biomolecular condensates in vitro, and the potential implications of these assemblies in bacterial resistance to antibiotic treatment.
Highlights
Resistance to antibiotics is already a major health threat and predicted to worsen unless new strategies are discovered to combat bacterial infections
Bacterial cell division is orchestrated by the divisome, a dynamic multiprotein complex that coordinates partitioning of daughter chromosomes, localized cell wall synthesis, and membrane invagination in order to achieve robust and reliable separation of daughter cells [2]
The search for new antibiotics active in bacterial division has mainly focused on FtsZ, because of its ubiquity and essential central role, and on the disruption of FtsZ
Summary
Resistance to antibiotics is already a major health threat and predicted to worsen unless new strategies are discovered to combat bacterial infections. The well characterized bacterial cell division machinery has lately attracted considerable attention in the quest for these new targets, as reflected by the growing number of reports on the subject [1] This high level of interest is spurred by the general conservation of cell division proteins in most bacterial species, clear differences from proteins involved in cytokinesis of animal cells, and emerging detailed understanding of the regulatory and structural mechanisms underlying the cell division process in several model bacterial systems. Among bacteria and archaea that carry it, FtsZ is largely conserved, with 40–50% sequence identity [6]; FtsZ orthologs are present in plastids This protein is a good for antimicrobials, both plastids algae and[1].
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