Isolation of a putative peroxidase, a target for factors controlling foot-formation in the coelenterate hydra

In hydra, differentiated ectodermal cells of the foot region contain a peroxidase activity that can be used as a marker for foot-specific differentiation processes. Because the expression of the gene coding for the peroxidase must be tightly regulated during foot-specific differentiation, characterization of the protein and cloning of the corresponding gene should provide valuable tools for getting deeper insights into the regulation of foot-specific differentiation. In this paper we characterize the foot-specific peroxidase by biochemical, histochemical, and molecular biological methods. We show that it is localized in granules, and that it consists of a single component, the molecular mass of which is in the range of 43-45 kDa. Purification of the protein and subsequent cloning of its complementary DNA yielded two closely related clones, ppod1 and ppod2 . Transcripts of ppod2 are abundant in the whole animal with the exception of the hypostome, the tentacles, and the foot; the expression of ppod1 matches exactly the localization of the foot-specific peroxidase.