Abstract
Ribosomal protein P0 is one of the highly conserved phosphorylated proteins in the large subunit of eukaryotic ribosomes. P0 has been shown in Drosophila to be a multifunctional protein that associates with elongation factor eEF2 to facilitate translation and also plays a role in DNA repair. In this paper we describe the cloning and characterization of the full-length cDNA encoding P0 from the mosquito, Aedes albopictus. In vitro translation showed that the cDNA encoded a 34kDa protein that corresponded in size to a phosphorylated protein from the large ribosomal subunit after in vivo labeling with [32P]orthophosphate. When cells were exposed to various stresses, expression of P0 appeared to differ from that of rpL34. Preliminary RNAi experiments suggested that downregulation of P0 is correlated with apoptosis in C7-10 mosquito cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1-10 |
| Number of pages | 10 |
| Journal | Genetica |
| Volume | 119 |
| Issue number | 1 |
| DOIs | |
| State | Published - Sep 2003 |
Bibliographical note
Funding Information:This work was supported by grants AI 20385 and AI 43971 from the National Institutes of Health, and by the University of Minnesota Agricultural Experiment Station, St. Paul, MN.
Keywords
- AP endonuclease
- Aedes albopictus
- Mosquito
- P0
- Ribosome