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dc.contributor.author
Freire, Miguel Angel
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dc.date.available
2017-04-27T21:33:29Z
dc.date.issued
2014-04
dc.identifier.citation
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
dc.identifier.issn
0735-9640
dc.identifier.uri
http://hdl.handle.net/11336/15815
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Potyvirus
dc.subject
Exosome
dc.subject
Nucleotidylylation
dc.subject
Rna Silencing
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.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
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-04-26T18:39:11Z
dc.identifier.eissn
1572-9818
dc.journal.volume
32
dc.journal.number
2
dc.journal.pagination
596-604
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Nueva York
dc.description.fil
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
dc.journal.title
Plant Molecular Biology Reporter
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s11105-013-0670-4
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s11105-013-0670-4
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