Qin, S. and Margolin, W. (1998). FtsZ dynamics during the division cycle of live Escherichia coli cells. J. Bacteriol. 180: 2050-2056.

Time-lapse fluorescence microscopy of FtsZ-GFP chimera protein expressed in E. coli demonstrating the dynamic nature of FtsZ localization, i.e. its assembly and disassembly as a ring at the cell midpoint, as well as at future division sites. This data is significant for two reasons: 1. It is the first real-time documentation of a prokaryotic structure-assembly process. 2. It demonstrated for the first time that Z ring assembly occurs early on in the cell cycle, as evidenced by the assembly of Z rings at the future division sites at the mother cell quarter positions.

Yu, X. and Margolin, W. (1997). The EMBO Journal. Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. 16: 5455-5463.

In vitro polymerization of FtsZ-GFP into asters, demonstrating the self-assembly properties of FtsZ. This process is dependent on the presence of GTP as well as Ca++. Interestingly, tubulin forms similar-looking asters in vitro.

Back to FtsZ Presentation

All Introduction Images and Schematics:

  • 1. Septum in a dividing cell (TEM).
  • 2. Schematic of FtsZ function during cell division.
  • 3. FtsL::GFP chimera protein localized as a ring in vivo.
  • 4. Time-lapse FtsZ localization and self-assembly.
  • 5. FtsZ/tubulin sequence alignment.
  • 6. Evolutionary history of FtsZ and tubulin.

    Animations used by permission of Dr. William Margolin , University of Texas Medical School.