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Diverse cell division components interact with FtsZ to regulate FtsZ assembly.
The widely conserved ZapA has been shown to interact with FtsZ, to drive its polymerisation and to promote FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring.
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In E. coli, two division proteins, ZipA and FtsA, directly interact with FtsZ and cooperate in anchoring FtsZ to the membrane (Pichoff & Lutkenhaus, 2002).
MinD is a membrane-associated ATPase that sequesters MinC to the membrane interface, allowing it to interact with FtsZ [25].
These results, combined with the observation that the intracellular ratio of ClpX to FtsZ is 1∶2, are consistent with a notion that in M. tuberculosis ClpX interacts with FtsZ at stoichiometric levels.
In view of its ability to interact with FtsZ, we name this gene product, FtsZ-interacting protein A (FipA).
On the other hand, the FipA (D118A) mutant retained the ability to interact with FtsZ.
Finally, two newly discovered cytoplasmic proteins, ZapA and ZapB, are found to interact with FtsZ and promote Z-ring assembly in vivo [51], [54], [61] [63].
FHA domain mutants S101A, H104A and N123A of FipA were impaired in their ability to interact with FtsZ in vivo (Fig. 2B).
As the F124S protein still forms rings, it is possible that this mutant is unable to interact with FtsZ.
To understand how ZapA might interact with FtsZ in nondividing cells and with the Z-ring in dividing cells, we performed the experiments at the physiological pH of 7.5 (41).
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