The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling
Autor(a) principal: | |
---|---|
Data de Publicação: | 2008 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.virol.2008.08.005 http://www.locus.ufv.br/handle/123456789/13866 |
Resumo: | 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. |
id |
UFV_3a617a5004133f801371003c2cbeb0c5 |
---|---|
oai_identifier_str |
oai:locus.ufv.br:123456789/13866 |
network_acronym_str |
UFV |
network_name_str |
LOCUS Repositório Institucional da UFV |
repository_id_str |
2145 |
spelling |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signalingBegomovirusAntiviral signalingNIK receptorRibosomal protein L10Receptor-like kinaseThe 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.Virology2017-11-28T10:39:12Z2017-11-28T10:39:12Z2008-08-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlepdfapplication/pdf00426822https://doi.org/10.1016/j.virol.2008.08.005http://www.locus.ufv.br/handle/123456789/13866engVolume 380, Issue 2, Pages 165-169, October 2008Rocha, Carolina S.Santos, Anésia A.Machado, João Paulo B.Fontes, Elizabeth P.B.info:eu-repo/semantics/openAccessreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFV2024-07-12T08:20:47Zoai:locus.ufv.br:123456789/13866Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452024-07-12T08:20:47LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.none.fl_str_mv |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
title |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
spellingShingle |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling Rocha, Carolina S. Begomovirus Antiviral signaling NIK receptor Ribosomal protein L10 Receptor-like kinase |
title_short |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
title_full |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
title_fullStr |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
title_full_unstemmed |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
title_sort |
The ribosomal protein L10/QM-like protein is a component of the NIK-mediated antiviral signaling |
author |
Rocha, Carolina S. |
author_facet |
Rocha, Carolina S. Santos, Anésia A. Machado, João Paulo B. Fontes, Elizabeth P.B. |
author_role |
author |
author2 |
Santos, Anésia A. Machado, João Paulo B. Fontes, Elizabeth P.B. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Rocha, Carolina S. Santos, Anésia A. Machado, João Paulo B. Fontes, Elizabeth P.B. |
dc.subject.por.fl_str_mv |
Begomovirus Antiviral signaling NIK receptor Ribosomal protein L10 Receptor-like kinase |
topic |
Begomovirus Antiviral signaling NIK receptor Ribosomal protein L10 Receptor-like kinase |
description |
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. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-08-02 2017-11-28T10:39:12Z 2017-11-28T10:39:12Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
00426822 https://doi.org/10.1016/j.virol.2008.08.005 http://www.locus.ufv.br/handle/123456789/13866 |
identifier_str_mv |
00426822 |
url |
https://doi.org/10.1016/j.virol.2008.08.005 http://www.locus.ufv.br/handle/123456789/13866 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Volume 380, Issue 2, Pages 165-169, October 2008 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
pdf application/pdf |
dc.publisher.none.fl_str_mv |
Virology |
publisher.none.fl_str_mv |
Virology |
dc.source.none.fl_str_mv |
reponame:LOCUS Repositório Institucional da UFV instname:Universidade Federal de Viçosa (UFV) instacron:UFV |
instname_str |
Universidade Federal de Viçosa (UFV) |
instacron_str |
UFV |
institution |
UFV |
reponame_str |
LOCUS Repositório Institucional da UFV |
collection |
LOCUS Repositório Institucional da UFV |
repository.name.fl_str_mv |
LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV) |
repository.mail.fl_str_mv |
fabiojreis@ufv.br |
_version_ |
1817560007558823936 |