Pr. Holden et al., CLONING AND CHARACTERIZATION OF AN FTSZ HOMOLOG FROM A BACTERIAL SYMBIONT OF DROSOPHILA-MELANOGASTER, MGG. Molecular & general genetics, 240(2), 1993, pp. 213-220
A 1194 bp open reading frame that codes for a 398 amino acid peptide w
as cloned from a lambdagt11 library of Drosophila melanogaster genomic
DNA. The predicted peptide sequence is very similar to three previous
ly characterized protein sequences that are encoded by the ftsZ genes
in Escherichia coli, Bacillus subtilis and Rhizobium meliloti. The Fts
Z protein has a major role in the initiation of cell division in proka
ryotic cells. Using a tetracycline treatment that eradicates bacterial
parasites from insects, the ftsZ homologue has been found to be deriv
ed from a bacterium that lives within the D. melanogaster strain. Howe
ver, polymerase chain reaction (PCR) amplification of the gene from tr
eated embryos suggests that it is not derived from a gut bacterium. Ne
vertheless, by amplifying and characterizing part of the 16S rRNA from
this bacterium we have been able to demonstrate that it is a member o
f the genus Wolbachia, a parasitic organism that infects, and disturbs
the sexual cycle of various strains of Drosophila simulans. We sugges
t that this ftsZ homologue is implicated in the cell division of Wolba
chia, an organism that fails to grow outside the host organism. Sequen
ce and alignment analysis of this ftsZ homologue show the presence of
a potential GTP-binding motif indicating that it may function as a GTP
ase. The consequences of this function particularly with respect to it
s role in cell division are discussed.