Abstract

Antibiotic resistances against bacterial diseases encouraged the design of novel and specific target based drugs. Screening of antibacterial agents against a specific target is an important strategy to develop novel inhibitors. FtsZ is a GTPase which orchestrates bacterial cytokinesis. FtsZ polymerizes in the presence of GTP and forms a contractile Z-ring at the mid of the bacterial cell which determines the plane of cell division. FtsZ assembly is highly dynamic in nature and it is tightly regulated by its interacting proteins known as regulators of FtsZ assembly. Some of these regulators promote the assembly of FtsZ protofilaments and stabilize the preformed protofilaments which lead to the formation of the divisome machinery complex known as positive regulators of FtsZ assembly. Contrary to the positive regulators, the negative regulators of the Z-ring assembly inhibit the formation of FtsZ protofilaments or destabilize the preformed protofilaments. The combined effect of both positive and negative regulators affects the localization of Z-ring during the bacterial cell division. FtsZ is a homologue of eukaryotic cytoskeleton protein tubulin, which is already used in cancer chemotherapy. Hence, the analysis of the mechanism of FtsZ assembly and exploring the interaction with its interacting proteins can help in designing FtsZ target based novel inhibitors.

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