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Comparative proteomics uncovers low asparagine content in Plasmodium tRip-KO proteins.
Pitolli, Martina; Cela, Marta; Kapps, Delphine; Chicher, Johana; Despons, Laurence; Frugier, Magali.
Affiliation
  • Pitolli M; Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, Strasbourg, France.
  • Cela M; Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, Strasbourg, France.
  • Kapps D; Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, Strasbourg, France.
  • Chicher J; Strasbourg-Esplanade Proteomics Facility, Université de Strasbourg, Strasbourg, France.
  • Despons L; Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, Strasbourg, France.
  • Frugier M; Université de Strasbourg, CNRS, Architecture et Réactivité de l'ARN, Strasbourg, France.
IUBMB Life ; 2024 Jul 04.
Article in En | MEDLINE | ID: mdl-38963319
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 downregulated 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.
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IUBMB Life / IUBMB life Journal subject: BIOLOGIA MOLECULAR / BIOQUIMICA Year: 2024 Type: Article Affiliation country: France

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IUBMB Life / IUBMB life Journal subject: BIOLOGIA MOLECULAR / BIOQUIMICA Year: 2024 Type: Article Affiliation country: France