Differential protein kinase C phosphorylation sites in the L17 ribosomal protein from Leishmania infantum

Leishmania infantum, the protozoan parasite responsible for leishmaniasis i n Europe, is capable of undergoing developmental changes in vitro and provi des an excellent model for the study of cell differentiation processes. We have cloned the gene encoding the L17 ribosomal protein. The LiL17 protein family belongs to the macrolide binding site, related to the peptidyl trans ferase center of the ribosome. its comparison with other members of the pro tein family shows several structural differences that may reflect functiona l variations. The protein kinase C phosphorylation sites display an interme diate pattern involving differences in location and type of residue with re spect to all the species considered. Gene-structural analysis suggests the existence of two different encoding genes. The expression of the genes seem to be different with the distinct growth phases of the parasite.