A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC

[EN] In most eukaryotes, RNA silencing is an adaptive immune system regulating key biological processes including antiviral defense. To evade this response, viruses of plants, worms and insects have evolved viral suppressors of RNA silencing proteins (VSRs). Various VSRs, such as P1 from Sweet potat...

Descripción completa

Detalles Bibliográficos
Autores: Kenesi, Erzsebet, Lozsa, Rita, Vertessy, Beata, Lakatos, Lorant, CARBONELL, ALBERTO|||0000-0001-5628-6632
Tipo de recurso: artículo
Fecha de publicación:2017
País:España
Institución:Universitat Politècnica de València (UPV)
Repositorio:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
Idioma:inglés
OAI Identifier:oai:riunet.upv.es:10251/161199
Acceso en línea:https://riunet.upv.es/handle/10251/161199
Access Level:acceso abierto
Palabra clave:RNA silencing
Plant virus, siRNA
AGO
Immunoprecipitation
Silencing suppressor
id ES_878c2af29db05d826bbdf57f71fddd97
oai_identifier_str oai:riunet.upv.es:10251/161199
network_acronym_str ES
network_name_str España
repository_id_str
spelling A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISCKenesi, ErzsebetLozsa, RitaVertessy, BeataLakatos, LorantCARBONELL, ALBERTO|||0000-0001-5628-6632RNA silencingPlant virus, siRNAAGOImmunoprecipitationSilencing suppressor[EN] In most eukaryotes, RNA silencing is an adaptive immune system regulating key biological processes including antiviral defense. To evade this response, viruses of plants, worms and insects have evolved viral suppressors of RNA silencing proteins (VSRs). Various VSRs, such as P1 from Sweet potato mild mottle virus (SPMMV), inhibit the activity of RNA-induced silencing complexes (RISCs) including an ARGONAUTE (AGO) protein loaded with a small RNA. However, the specific mechanisms explaining this class of inhibition are unknown. Here, we show that SPMMV P1 interacts with AGO1 and AGO2 from Arabidopsis thaliana, but solely interferes with AGO1 function. Moreover, a mutational analysis of a newly identified zinc finger domain in P1 revealed that this domain could represent an effector domain as it is required for P1 suppressor activity but not for AGO1 binding. Finally, a comparative analysis of the target RNA binding capacity of AGO1 in the presence of wild-type or suppressor-defective P1 forms revealed that P1 blocks target RNA binding to AGO1. Our results describe the negative regulation of RISC, the small RNA containing molecular machine.Hungarian Scientific Research Fund (OTKA) [K91042, NN107787, NN11024 to L.L.]; European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska Curie [655841 to A.C.]. Funding for open access charge: OTKA [NN11024]Oxford University PressInstituto Universitario Mixto de Biología Molecular y Celular de PlantasHungarian Scientific Research FundEuropean CommissionRepositorio Institucional de la Universitat Politècnica de València Riunet20172017-07-27journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://riunet.upv.es/handle/10251/161199reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valénciainstname:Universitat Politècnica de València (UPV)InglésengEuropean Commission https://doi.org/10.13039/501100000780 H2020 655841 Genome-wide analysis of RNA and protein interacting profiles during a plant virus infectionHungarian Scientific Research Fund https://doi.org/10.13039/501100003549 K91042Hungarian Scientific Research Fund https://doi.org/10.13039/501100003549 NN107787Hungarian Scientific Research Fund https://doi.org/10.13039/501100003549 NN11024open accesshttp://purl.org/coar/access_right/c_abf2Reconocimiento (by)http://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:riunet.upv.es:10251/1611992026-06-13T07:49:27Z
dc.title.none.fl_str_mv A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
title A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
spellingShingle A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
Kenesi, Erzsebet
RNA silencing
Plant virus, siRNA
AGO
Immunoprecipitation
Silencing suppressor
title_short A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
title_full A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
title_fullStr A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
title_full_unstemmed A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
title_sort A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC
dc.creator.none.fl_str_mv Kenesi, Erzsebet
Lozsa, Rita
Vertessy, Beata
Lakatos, Lorant
CARBONELL, ALBERTO|||0000-0001-5628-6632
author Kenesi, Erzsebet
author_facet Kenesi, Erzsebet
Lozsa, Rita
Vertessy, Beata
Lakatos, Lorant
CARBONELL, ALBERTO|||0000-0001-5628-6632
author_role author
author2 Lozsa, Rita
Vertessy, Beata
Lakatos, Lorant
CARBONELL, ALBERTO|||0000-0001-5628-6632
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Instituto Universitario Mixto de Biología Molecular y Celular de Plantas
Hungarian Scientific Research Fund
European Commission
Repositorio Institucional de la Universitat Politècnica de València Riunet
dc.subject.none.fl_str_mv RNA silencing
Plant virus, siRNA
AGO
Immunoprecipitation
Silencing suppressor
topic RNA silencing
Plant virus, siRNA
AGO
Immunoprecipitation
Silencing suppressor
description [EN] In most eukaryotes, RNA silencing is an adaptive immune system regulating key biological processes including antiviral defense. To evade this response, viruses of plants, worms and insects have evolved viral suppressors of RNA silencing proteins (VSRs). Various VSRs, such as P1 from Sweet potato mild mottle virus (SPMMV), inhibit the activity of RNA-induced silencing complexes (RISCs) including an ARGONAUTE (AGO) protein loaded with a small RNA. However, the specific mechanisms explaining this class of inhibition are unknown. Here, we show that SPMMV P1 interacts with AGO1 and AGO2 from Arabidopsis thaliana, but solely interferes with AGO1 function. Moreover, a mutational analysis of a newly identified zinc finger domain in P1 revealed that this domain could represent an effector domain as it is required for P1 suppressor activity but not for AGO1 binding. Finally, a comparative analysis of the target RNA binding capacity of AGO1 in the presence of wild-type or suppressor-defective P1 forms revealed that P1 blocks target RNA binding to AGO1. Our results describe the negative regulation of RISC, the small RNA containing molecular machine.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017-07-27
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://riunet.upv.es/handle/10251/161199
url https://riunet.upv.es/handle/10251/161199
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv European Commission https://doi.org/10.13039/501100000780 H2020 655841 Genome-wide analysis of RNA and protein interacting profiles during a plant virus infection
Hungarian Scientific Research Fund https://doi.org/10.13039/501100003549 K91042
Hungarian Scientific Research Fund https://doi.org/10.13039/501100003549 NN107787
Hungarian Scientific Research Fund https://doi.org/10.13039/501100003549 NN11024
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reconocimiento (by)
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reconocimiento (by)
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname:Universitat Politècnica de València (UPV)
instname_str Universitat Politècnica de València (UPV)
reponame_str RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
collection RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869412469804367872
score 15,301603

Similares en LA Referencia