Date of Degree
Bacteriology | Biochemistry | Bioinformatics | Cell Biology | Molecular Biology | Molecular Genetics
E. coli cytokinesis, FtsZ, FtsZ CTV region, ZapC, ZapD, CCTP
An essential first step in bacterial division is the assembly of a cytokinetic ring (Z-ring) formed by the tubulin-like FtsZ at midcell. The highly conserved core domain of FtsZ has been reported to mediate assembly of FtsZ polymers in vivo and in vitro. Species-specific differences in the FtsZ C-terminal domain such as the FtsZ CTV region and interactions with several modulatory proteins such as ZapC and ZapD, restricted to certain bacterial classes, also serve as key determinants of FtsZ protofilament bundling. Here, we characterize (i) the roles of the FtsZ CTV region in mediating both longitudinal and lateral interactions of FtsZ polymers and their impacts on Z-ring assembly in E. coli, and (ii) the structure-function relationship of FtsZ with two regulators, ZapC and ZapD, which have no primary sequence homology but have overlapping functions in Z-ring assembly and stability in E. coli. This work is expected to provide significant insight into the roles of different FtsZ domain sequences on the assembly of dynamic FtsZ polymers as well as the roles of modulatory proteins in mediating the assembly of an efficient cytokinetic ring during the early stage of E. coli cytokinesis.
Huang, Kuo-Hsiang, "Molecular Analysis of FtsZ-Ring Assembly in E. coli cytokinesis" (2016). CUNY Academic Works.