A recombinant plasmid L4440-GTU expressing γ-tubulin dsRNA of the ciliate Euplotes eurystomus was constructed and transferred into Escherichia coli strain HT115. The resultant E. coli bacteria were fed on E. eurystomus to inhibit the ciliate's γ-tubulin gene expression. As a result, the γ-tubulin gene expression level was decreased, and this inactivation blocked cell division, which was lethal. In addition, the loss of the C-tubule from the nine-microtubule triplets in basal bodies, and the disappearance of some microtubules or mislocalization of some microtubule organization units in the subpellicular microtubule layers were also observed. These results indicate that the γ-tubulin is not only important for the stability of the nine-microtubule triplets in basal bodies, but also necessary for the integrity of microtubule organization patterns in the subpellicular microtubule layer.