Deinococcus radiodurans is radioresistant and grows with a doubling time of 90 min.
FtsZ level is same during postirradiation recovery but growth gets arrested in response to gamma radiation.
Recombinant FtsZDr is a GTPase with slower rate of polymerization than E. coli but faster than Mycobacterial FtsZ.
FtsZDr forms typical Z ring in vivo.
The GTPase-dependent polymerization/depolymerization dynamics of FtsZ regulate bacterial cell division in vivo. Deinococcus radiodurans is better known for its extraordinary radioresistance and therefore, the characterization of FtsZ of this bacterium (FtsZDr) would be required to understand the mechanisms underlying regulation of cell division in response to DNA damage. Recombinant FtsZDr bound to GTP and showed GTPase activity. It produced bundles of protofilaments in the presence of either GTP or Mg2+ ions. But the formation of the higher size ordered structures required both GTP and Mg2+in vitro. It showed polymerization/depolymerization dynamics as a function of GTP and Mg2+. Interestingly, ATP interacted with FtsZDr and stimulated its GTPase activity by ∼2-fold possibly by increasing both substrate affinity and rate of reaction. FtsZDr-GFP expressing in D. radiodurans produced typical Z ring perpendicular to the plane of first cell division. These results suggested that FtsZDr is a GTPase in vitro and produces typical Z ring at the mid cell position in D. radiodurans.
KeywordsBacterial cell division
; Protein polymerization