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 |
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Přispěvatelé: | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, Universidad de Sevilla |
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Genetics Apicoplast 030102 biochemistry & molecular biology biology RNA recognition motif Plasmodium vivax RNA RNA-binding protein biology.organism_classification Apicoplast RNA binding protein General Biochemistry Genetics and Molecular Biology 3. Good health Apicomplexa 03 medical and health sciences 030104 developmental biology parasitic diseases Protein biosynthesis Malarial Plasmodium parasite Plastid Protein aggregation |
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 |
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