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Campo DC | Valor | Idioma |
---|---|---|
dc.contributor.author | Rocha, Carolina S. | |
dc.contributor.author | Santos, Anésia A. | |
dc.contributor.author | Machado, João Paulo B. | |
dc.contributor.author | Fontes, Elizabeth P.B. | |
dc.date.accessioned | 2017-11-28T10:39:12Z | |
dc.date.available | 2017-11-28T10:39:12Z | |
dc.date.issued | 2008-08-02 | |
dc.identifier.issn | 00426822 | |
dc.identifier.uri | https://doi.org/10.1016/j.virol.2008.08.005 | |
dc.identifier.uri | http://www.locus.ufv.br/handle/123456789/13866 | |
dc.description.abstract | The NIK (NSP-interacting kinase)-mediated antiviral signaling pathway was identified as a virulence target of the begomovirus nuclear shuttle protein (NSP). Here, we further characterized this layer of plant innate defense by identifying the ribosomal protein L10 (rpL10), a QM-like protein, as a downstream effector of the antiviral signaling. Although both ribosomal proteins rpL10 and rpL18 were found to associate with NIK1 through yeast two-hybrid screening, the NIK receptors specifically phosphorylated rpL10 in vitro. Furthermore, loss of rpL10 function significantly increased susceptibility to begomovirus infection, recapitulating the phenotype of nik knockout lines. Our results genetically linked rpL10 to the NIK-mediated antiviral signaling. | en |
dc.format | pt-BR | |
dc.language.iso | eng | pt-BR |
dc.publisher | Virology | pt-BR |
dc.relation.ispartofseries | Volume 380, Issue 2, Pages 165-169, October 2008 | pt-BR |
dc.rights | Open Access | pt-BR |
dc.subject | Begomovirus | pt-BR |
dc.subject | Antiviral signaling | pt-BR |
dc.subject | NIK receptor | pt-BR |
dc.subject | Ribosomal protein L10 | pt-BR |
dc.subject | Receptor-like kinase | pt-BR |
dc.title | The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling | en |
dc.type | Artigo | pt-BR |
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