Bacterial cell division depends on the formation of a cytokinetic ring stru
cture, the Z-ring. The bacterial tubulin homologue FtsZ is required for Z-r
ing formation. FtsZ assembles into various polymeric forms in vitro, indica
ting a structural role in the septum of bacteria. We have used recombinant
FtsZ1 protein from M. jannaschii to produce helical tubes a nd sheets with
high yield using the GTP analogue GM PC PP [guanylyl (alpha,beta)-methylene
-diphosphate]. The sheets appear identical to the previously reported Ca++-
induced sheets of FtsZ from M. jannaschii that were shown to consist of 'th
ick'-filaments in which two protofilaments run in parallel. Tubes assembled
either in Ca++ or in GMPCPP contain filaments whose dimensions indicate th
at they could be equivalent to the 'thick'-filaments in sheets. Some tubes
are hollow but others are filled by additional protein density. Helical Fts
Z tubes differ from eukaryotic microtubules in that the filaments curve aro
und the filament axis with a pitch of similar to 430 Angstrom for Ca++-indu
ced tubes or 590 - 620 Angstrom for GMPCPP. However, their assembly in vitr
o as well-ordered polymers over distances comparable to the inner circumfer
ence of a bacterium may indicate a role in vivo. Their size and stability m
ake them suitable for use in motility assays.