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J Biol Chem, Vol. 273, Issue 17, 10216-10222, April 24, 1998
From the Department of Microbiology and Molecular Genetics,
University of Texas Medical School, Houston, Texas 77030
To gain further insight into the structural
relatedness of tubulin and FtsZ, the tubulin-like prokaryotic cell
division protein, we tested the effect of tubulin assembly inhibitors
on FtsZ assembly. Common tubulin inhibitors, such as colchicine,
colcemid, benomyl, and vinblastine, had no effect on
Ca2+-promoted GTP-dependent assembly of
FtsZ into polymers. However, the hydrophobic probe
5,5'-bis-(8-anilino-1-naphthalenesulfonate) (bis-ANS) inhibited FtsZ
assembly. The potential mechanisms for inhibition are discussed.
Titrations of FtsZ with bis-ANS indicated that FtsZ has one high
affinity binding site and multiple low affinity binding sites. ANS
(8-anilino-1-naphthalenesulfonate), a hydrophobic probe similar to
bis-ANS, had no inhibitory effect on FtsZ assembly. Because tubulin
assembly has also been shown to be inhibited by bis-ANS but not by ANS,
it supports the idea that FtsZ and tubulin share similar conformational
properties. Ca2+, which promotes GTP-dependent
FtsZ assembly, stimulated binding of bis-ANS or ANS to FtsZ, suggesting
that Ca2+ binding induces changes in the hydrophobic
conformation of the protein. Interestingly, depletion of bound
Ca2+ with EGTA further enhanced bis-ANS fluorescence. These
findings suggest that both binding and dissociation of Ca2+
are capable of inducing FtsZ conformational changes, and these changes
could promote the GTP-dependent assembly of FtsZ.
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