A putative RNA binding protein from Plasmodium vivax apicoplast

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...

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Autores: García Mauriño, Sofía M., Díaz Quintana, Antonio Jesús, Rivero Rodríguez, Francisco, Cruz Gallardo, Isabel, Grüttner, Christian, Hernández Vellisca, Marian, Díaz Moreno, Irene
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/70344
Acceso en línea:https://hdl.handle.net/11441/70344
https://doi.org/10.1002/2211-5463.12351
Access Level:acceso abierto
Palabra clave:apicoplast RNA binding protein
malarial Plasmodium parasite
protein aggregation
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spelling A putative RNA binding protein from Plasmodium vivax apicoplastGarcía Mauriño, Sofía M.Díaz Quintana, Antonio JesúsRivero Rodríguez, FranciscoCruz Gallardo, IsabelGrüttner, ChristianHernández Vellisca, MarianDíaz Moreno, Ireneapicoplast RNA binding proteinmalarial Plasmodium parasiteprotein aggregationMalaria 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.Junta de Andalucía P11-CVI-7216 and BIO-198Universidad de Sevilla VI PPIT-USWileyBioquímica Vegetal y Biología MolecularJunta de AndalucíaUniversidad de Sevilla2018info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/70344https://doi.org/10.1002/2211-5463.12351reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésFEBS Open Bio, 8 (2), 177-188.P11-CVI-7216http://dx.doi.org/10.1002/2211-5463.12351info:eu-repo/semantics/openAccessoai:idus.us.es:11441/703442026-06-17T12:51:07Z
dc.title.none.fl_str_mv A putative RNA binding protein from Plasmodium vivax apicoplast
title A putative RNA binding protein from Plasmodium vivax apicoplast
spellingShingle A putative RNA binding protein from Plasmodium vivax apicoplast
García Mauriño, Sofía M.
apicoplast RNA binding protein
malarial Plasmodium parasite
protein aggregation
title_short A putative RNA binding protein from Plasmodium vivax apicoplast
title_full A putative RNA binding protein from Plasmodium vivax apicoplast
title_fullStr A putative RNA binding protein from Plasmodium vivax apicoplast
title_full_unstemmed A putative RNA binding protein from Plasmodium vivax apicoplast
title_sort A putative RNA binding protein from Plasmodium vivax apicoplast
dc.creator.none.fl_str_mv García Mauriño, Sofía M.
Díaz Quintana, Antonio Jesús
Rivero Rodríguez, Francisco
Cruz Gallardo, Isabel
Grüttner, Christian
Hernández Vellisca, Marian
Díaz Moreno, Irene
author García Mauriño, Sofía M.
author_facet García Mauriño, Sofía M.
Díaz Quintana, Antonio Jesús
Rivero Rodríguez, Francisco
Cruz Gallardo, Isabel
Grüttner, Christian
Hernández Vellisca, Marian
Díaz Moreno, Irene
author_role author
author2 Díaz Quintana, Antonio Jesús
Rivero Rodríguez, Francisco
Cruz Gallardo, Isabel
Grüttner, Christian
Hernández Vellisca, Marian
Díaz Moreno, Irene
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Junta de Andalucía
Universidad de Sevilla
dc.subject.none.fl_str_mv apicoplast RNA binding protein
malarial Plasmodium parasite
protein aggregation
topic apicoplast RNA binding protein
malarial Plasmodium parasite
protein aggregation
description 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.
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/70344
https://doi.org/10.1002/2211-5463.12351
url https://hdl.handle.net/11441/70344
https://doi.org/10.1002/2211-5463.12351
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv FEBS Open Bio, 8 (2), 177-188.
P11-CVI-7216
http://dx.doi.org/10.1002/2211-5463.12351
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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