Differential protein kinase C phosphorylation sites in the L17 ribosomal protein from Leishmania infantum.
Leishmania infantum, the protozoan parasite responsible for leishmaniasis in Europe, is capable of undergoing developmental changes in vitro and provides 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 transferase center of the ribosome. Its comparison with other members of the protein family shows several structural differences that may reflect functional variations. The protein kinase C phosphorylation sites display an intermediate pattern involving differences in location and type of residue with respect 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.
Gonzalez-Aseguinolaza
G
G
Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Taladriz
S
S
Marquet
A
A
Larraga
V
V
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D003001:Cloning, Molecular; D018076:DNA, Complementary; D018314:Leishmania infantum / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D018076:DNA, Complementary; D012269:Ribosomal Proteins; C032493:ribosomal protein L17; D011493:Protein Kinase C