抄録
Porphyromonas gingivalis is an oral anaerobic rod-shaped bacterium, involved in periodontal diseases. The cell division gene, ftsZ, has been cloned from P. gingivalis 381. This gene encoded a protein of 458 amino acids with a deduced molecular weight of 50.3kDa, as confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Like other eubacterial homologues, P. gingivalis FtsZ possesses a putative GTP binding motif and a GTP hydrolyzing region. Although P. gingivalis ftsZ could not complement an Escherichia coli ftsZ mutant, overproduction of P. gingivalis FtsZ in E. coli resulted in the formation of long filamentous cells. To assess P. gingivalis FtsZ function as a GTPase, the FtsZ proteins were partly purified, examined GTPase activity using 2-amino-6-mercapto-7-methylpurine ribonucleoside (MESG)/phosphorylase system, and determined a GTPase activity. This was suggested that P. gingivalis FtsZ may be also shared universal characteristics among FtsZs.
