bioRxivBiochemistryPreprint
Comparative proteomics uncovers low asparagine insertion in Plasmodium tRip-KO proteins.
M. Pitolli, M. Cela, D. Kapps, J. Chicher, L. Despons, M. Frugier
Abstract
tRNAs are not only essential for decoding the genetic code, but their abundance also has a strong impact on the rate of protein production, folding, and on the stability of the translated messenger RNAs. Plasmodium expresses a unique surface protein called tRip, involved in the import of exogenous tRNAs into the parasite. Comparative proteomic analysis of the blood stage of wild-type and tRip-KO variant of P. berghei parasites revealed that down-regulated proteins in the mutant parasite are distinguished by a bias in their asparagine content. Furthermore, the demonstration of the possibility of charging host tRNAs with Plasmodium aminoacyl-tRNA synthetases, led us to propose that, imported host tRNAs participate in parasite protein synthesis. These results also suggest a novel mechanism of translational control in which import of host tRNAs emerge as regulators of gene expression in the Plasmodium developmental cycle and pathogenesis, by enabling the synthesis of asparagine-rich regulatory proteins that efficiently and selectively control the parasite infectivity.
- organism: plant (other)
- assay: proteomics
- research focus: cell type annotation
- research focus: protein folding & dynamics
- research focus: host-pathogen & immune response
- approach: experimental assay
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