A putative RNA binding protein from Plasmodium vivax apicoplast

Autor: Christian Grüttner, Sofía García-Mauriño, Isabel Cruz-Gallardo, Marian Hernández-Vellisca, Francisco Rivero-Rodríguez, Irene Díaz-Moreno, Antonio Díaz-Quintana
Přispěvatelé: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, Universidad de Sevilla
Rok vydání: 2018
Předmět:
Zdroj: Digital.CSIC. Repositorio Institucional del CSIC
instname
idUS. Depósito de Investigación de la Universidad de Sevilla
Popis: Malaria is caused by Apicomplexa protozoans from the Plasmodium genus entering the bloodstream of humans and animals through the bite of the female mosquitoes. The annotation of the Plasmodium vivax genome revealed a putative RNA binding protein (apiRBP) that was predicted to be trafficked into the apicoplast, a plastid organelle unique to Apicomplexa protozoans. Although a 3D structural model of the apiRBP corresponds to a noncanonical RNA recognition motif with an additional C-terminal ¿-helix (¿3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering ¿3. Hence, we used a C-terminal GFP-fused chimera to stabilize the highly insoluble apiRBP and determined its ability to bind U-rich stretches of RNA. The affinity of apiRBP toward such RNAs is highly dependent on ionic strength, suggesting that the apiRBP-RNA complex is driven by electrostatic interactions. Altogether, apiRBP represents an attractive tool for apicoplast transcriptional studies and for antimalarial drug design.
Databáze: OpenAIRE