Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein

Autores
Freire, Miguel Angel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The helper-component proteinase (HC-Pro) of potyvirus is a multifunctional protein involved in many mechanisms of viral life cycle. In addition, HC-Pro protein was the first identified suppressor of RNA silencing in plants. However, the identities and functions of direct targets toward the pathways of RNA-silencing suppression mediated by HC-Pro are still to be determined. Here, a yeast two-hybrid search for potyviral HC-Pro interacting tobacco proteins was done to identify host partners and potential silencing suppressors. Two interacting cDNA clones were isolated. One of them encodes an Rrp6-like protein, a subunit of the exosome complex that belongs to the RNase D family of the DEDD superfamily of 3′–5′ hydrolytic exoribonucleases. The other clone codes for a small α-heat shock protein (α-Hsp). The interactions were validated by cross interaction assays with other potyviral HC-Pro proteins. Moreover, both identified clones also interacted with pathogenic viral protein-linked genomes (VPgs) and with translation eukaryotic initiation factors (iso) 4E (eIF(iso)4E) which are host determinants of resistance or susceptibility to potyvirus infections. All together, these findings emphasize the role of the potyviral HC-Pro and VPg proteins and the translation initiation factor eIF(iso)4E, as key players of the plant–virus interplay, where the exoribonuclease Rrp6 and a small α-heat shock protein appear as novel sharing targets.
Fil: Freire, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Materia
Potyvirus
Exosome
Nucleotidylylation
Rna Silencing
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/15815
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/15815
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock proteinFreire, Miguel AngelPotyvirusExosomeNucleotidylylationRna Silencinghttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The helper-component proteinase (HC-Pro) of potyvirus is a multifunctional protein involved in many mechanisms of viral life cycle. In addition, HC-Pro protein was the first identified suppressor of RNA silencing in plants. However, the identities and functions of direct targets toward the pathways of RNA-silencing suppression mediated by HC-Pro are still to be determined. Here, a yeast two-hybrid search for potyviral HC-Pro interacting tobacco proteins was done to identify host partners and potential silencing suppressors. Two interacting cDNA clones were isolated. One of them encodes an Rrp6-like protein, a subunit of the exosome complex that belongs to the RNase D family of the DEDD superfamily of 3′–5′ hydrolytic exoribonucleases. The other clone codes for a small α-heat shock protein (α-Hsp). The interactions were validated by cross interaction assays with other potyviral HC-Pro proteins. Moreover, both identified clones also interacted with pathogenic viral protein-linked genomes (VPgs) and with translation eukaryotic initiation factors (iso) 4E (eIF(iso)4E) which are host determinants of resistance or susceptibility to potyvirus infections. All together, these findings emphasize the role of the potyviral HC-Pro and VPg proteins and the translation initiation factor eIF(iso)4E, as key players of the plant–virus interplay, where the exoribonuclease Rrp6 and a small α-heat shock protein appear as novel sharing targets.Fil: Freire, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaSpringer2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/15815Freire, Miguel Angel; Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein; Springer; Plant Molecular Biology Reporter; 32; 2; 4-2014; 596-6040735-96401572-9818enginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s11105-013-0670-4info:eu-repo/semantics/altIdentifier/doi/10.1007/s11105-013-0670-4info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:06Zoai:ri.conicet.gov.ar:11336/15815instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:04:06.381CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
title Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
spellingShingle Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
Freire, Miguel Angel
Potyvirus
Exosome
Nucleotidylylation
Rna Silencing
title_short Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
title_full Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
title_fullStr Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
title_full_unstemmed Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
title_sort Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein
dc.creator.none.fl_str_mv Freire, Miguel Angel
author Freire, Miguel Angel
author_facet Freire, Miguel Angel
author_role author
dc.subject.none.fl_str_mv Potyvirus
Exosome
Nucleotidylylation
Rna Silencing
topic Potyvirus
Exosome
Nucleotidylylation
Rna Silencing
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The helper-component proteinase (HC-Pro) of potyvirus is a multifunctional protein involved in many mechanisms of viral life cycle. In addition, HC-Pro protein was the first identified suppressor of RNA silencing in plants. However, the identities and functions of direct targets toward the pathways of RNA-silencing suppression mediated by HC-Pro are still to be determined. Here, a yeast two-hybrid search for potyviral HC-Pro interacting tobacco proteins was done to identify host partners and potential silencing suppressors. Two interacting cDNA clones were isolated. One of them encodes an Rrp6-like protein, a subunit of the exosome complex that belongs to the RNase D family of the DEDD superfamily of 3′–5′ hydrolytic exoribonucleases. The other clone codes for a small α-heat shock protein (α-Hsp). The interactions were validated by cross interaction assays with other potyviral HC-Pro proteins. Moreover, both identified clones also interacted with pathogenic viral protein-linked genomes (VPgs) and with translation eukaryotic initiation factors (iso) 4E (eIF(iso)4E) which are host determinants of resistance or susceptibility to potyvirus infections. All together, these findings emphasize the role of the potyviral HC-Pro and VPg proteins and the translation initiation factor eIF(iso)4E, as key players of the plant–virus interplay, where the exoribonuclease Rrp6 and a small α-heat shock protein appear as novel sharing targets.
Fil: Freire, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
description The helper-component proteinase (HC-Pro) of potyvirus is a multifunctional protein involved in many mechanisms of viral life cycle. In addition, HC-Pro protein was the first identified suppressor of RNA silencing in plants. However, the identities and functions of direct targets toward the pathways of RNA-silencing suppression mediated by HC-Pro are still to be determined. Here, a yeast two-hybrid search for potyviral HC-Pro interacting tobacco proteins was done to identify host partners and potential silencing suppressors. Two interacting cDNA clones were isolated. One of them encodes an Rrp6-like protein, a subunit of the exosome complex that belongs to the RNase D family of the DEDD superfamily of 3′–5′ hydrolytic exoribonucleases. The other clone codes for a small α-heat shock protein (α-Hsp). The interactions were validated by cross interaction assays with other potyviral HC-Pro proteins. Moreover, both identified clones also interacted with pathogenic viral protein-linked genomes (VPgs) and with translation eukaryotic initiation factors (iso) 4E (eIF(iso)4E) which are host determinants of resistance or susceptibility to potyvirus infections. All together, these findings emphasize the role of the potyviral HC-Pro and VPg proteins and the translation initiation factor eIF(iso)4E, as key players of the plant–virus interplay, where the exoribonuclease Rrp6 and a small α-heat shock protein appear as novel sharing targets.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/15815
Freire, Miguel Angel; Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein; Springer; Plant Molecular Biology Reporter; 32; 2; 4-2014; 596-604
0735-9640
1572-9818
url http://hdl.handle.net/11336/15815
identifier_str_mv Freire, Miguel Angel; Potyviral VPg and HC-Pro proteins and the cellular translation initiation factor eIF(iso)4E interact with exoribonuclease Rrp6 and a small a-heat shock protein; Springer; Plant Molecular Biology Reporter; 32; 2; 4-2014; 596-604
0735-9640
1572-9818
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s11105-013-0670-4
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11105-013-0670-4
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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