Characterization of the ribosomal proteins from mosquito (Aedes albopictus) cells.
Proteins from the large and small subunits of Aedes albopictus (mosquito) cytoplasmic ribosomes were characterized by two-dimensional polyacrylamide gel electrophoresis. The small subunit contained 28-31 proteins ranging in molecular mass from 10 to 49 kDa. The large subunit contained 36-39 proteins that ranged in molecular mass from 11 to 53 kDa. The largest protein on the small subunit, S1, was the predominant phosphorylated ribosomal protein. Under long-term labelling conditions, L4 and L33 were also phosphorylated. Peptide mapping by partial proteolysis indicated that Ae. albopictus S1 may share partial amino acid homology with the phosphorylated ribosomal protein S6 from Drosophila melanogaster. Unlike Drosophila S6, however, Aedes S1 was not dephosphorylated during heat shock. Treatment of mosquito cells with the insect molting hormone 20-hydroxyecdysone did not affect phosphorylation of ribosomal proteins.
D000330:Aedes / Q000032:analysis*; D000818:Animals; D001345:Autoradiography; D004331:Drosophila melanogaster / Q000032:analysis; D004441:Ecdysterone / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008970:Molecular Weight; D010766:Phosphorylation; D012269:Ribosomal Proteins / Q000032:analysis*
D012269:Ribosomal Proteins; D004441:Ecdysterone