A putative RNA binding protein from Plasmodium vivax apicoplast

Sofía M. García-Mauriño; Antonio Díaz-Quintana; Francisco Rivero-Rodríguez; Isabel Cruz-Gallardo; Christian Grüttner; Marian Hernández-Vellisca; Irene Díaz-Moreno

doi:10.1002/2211-5463.12351

A putative RNA binding protein from Plasmodium vivax apicoplast

Sofía M. García-Mauriño, Antonio Díaz-Quintana, Francisco Rivero-Rodríguez, Isabel Cruz-Gallardo, Christian Grüttner, Marian Hernández-Vellisca, Irene Díaz-Moreno^*

^*Corresponding author for this work

Randall Centre of Cell & Molecular Biophysics

CSIC-JA-USE - Centro de Investigaciones Cient&iacute;ficas Isla de la Cartuja (CICIC)

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

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 α-helix (α₃), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α₃. 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.

Original language	English
Journal	FEBS Open Bio
Early online date	31 Dec 2017
DOIs	https://doi.org/10.1002/2211-5463.12351
Publication status	E-pub ahead of print - 31 Dec 2017

Keywords

Apicoplast RNA binding protein
Malarial Plasmodium parasite
Protein aggregation

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/2211-5463.12351Licence: CC BY

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title = "A putative RNA binding protein from Plasmodium vivax apicoplast",

abstract = "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 α-helix (α3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α3. 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.",

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T1 - A putative RNA binding protein from Plasmodium vivax apicoplast

AU - García-Mauriño, Sofía M.

AU - Díaz-Quintana, Antonio

AU - Rivero-Rodríguez, Francisco

AU - Cruz-Gallardo, Isabel

AU - Grüttner, Christian

AU - Hernández-Vellisca, Marian

AU - Díaz-Moreno, Irene

PY - 2017/12/31

Y1 - 2017/12/31

N2 - 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 α-helix (α3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α3. 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.

AB - 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 α-helix (α3), preliminary protein production trials were nevertheless unsuccessful. Theoretical solvation analysis of the apiRBP model highlighted an exposed hydrophobic region clustering α3. 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.

KW - Apicoplast RNA binding protein

KW - Malarial Plasmodium parasite

KW - Protein aggregation

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M3 - Article

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A putative RNA binding protein from Plasmodium vivax apicoplast

Abstract

Keywords

UN SDGs

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