Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity

Autores
Modena, Natalia Andrea; Zelada, Alicia Mercedes; Conte, Ana Florencia; Mentaberry, Alejandro Nestor
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection.
Fil: Modena, Natalia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Zelada, Alicia Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Conte, Ana Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Mentaberry, Alejandro Nestor. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Materia
Ck2
Phosphorylation
Pvx
Triple Gene Block
Viral Mobilization
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:11336/79706
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79706
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activityModena, Natalia AndreaZelada, Alicia MercedesConte, Ana FlorenciaMentaberry, Alejandro NestorCk2PhosphorylationPvxTriple Gene BlockViral Mobilizationhttps://purl.org/becyt/ford/4.4https://purl.org/becyt/ford/4https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection.Fil: Modena, Natalia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Zelada, Alicia Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Conte, Ana Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Mentaberry, Alejandro Nestor. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaElsevier Science2008-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79706Modena, Natalia Andrea; Zelada, Alicia Mercedes; Conte, Ana Florencia; Mentaberry, Alejandro Nestor; Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity; Elsevier Science; Virus Research; 137; 1; 10-2008; 16-230168-1702CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/18632176info:eu-repo/semantics/altIdentifier/doi/10.1016/j.virusres.2008.04.007info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168170208001408info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:56Zoai:ri.conicet.gov.ar:11336/79706instacron: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 10:08:56.316CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
title Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
spellingShingle Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
Modena, Natalia Andrea
Ck2
Phosphorylation
Pvx
Triple Gene Block
Viral Mobilization
title_short Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
title_full Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
title_fullStr Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
title_full_unstemmed Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
title_sort Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity
dc.creator.none.fl_str_mv Modena, Natalia Andrea
Zelada, Alicia Mercedes
Conte, Ana Florencia
Mentaberry, Alejandro Nestor
author Modena, Natalia Andrea
author_facet Modena, Natalia Andrea
Zelada, Alicia Mercedes
Conte, Ana Florencia
Mentaberry, Alejandro Nestor
author_role author
author2 Zelada, Alicia Mercedes
Conte, Ana Florencia
Mentaberry, Alejandro Nestor
author2_role author
author
author
dc.subject.none.fl_str_mv Ck2
Phosphorylation
Pvx
Triple Gene Block
Viral Mobilization
topic Ck2
Phosphorylation
Pvx
Triple Gene Block
Viral Mobilization
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.4
https://purl.org/becyt/ford/4
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection.
Fil: Modena, Natalia Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Zelada, Alicia Mercedes. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Conte, Ana Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Mentaberry, Alejandro Nestor. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
description The movement protein (MP) TGBp1 of the potexvirus Potato virus X (PVX) is a multifunctional protein required for cell-to-cell movement within the host plant. Recent work on other plant viruses has indicated that MP phosphorylation by host kinases can regulate MP function. In this study, we demonstrate that recombinant and native TGBp1 are phosphorylated by Nicotiana tabacum extracts from both PVX-infected and non-infected leaves. The phosphorylation activity present in plant extracts has distinctive characteristics of casein kinase 2 (CK2): it is inhibited by heparin, stimulated by polylysine, and uses either ATP or GTP as phosphoryl donors. We also demonstrate that TGBp1 is efficiently phosphorylated by recombinant tobacco CK2 α subunit and by partially purified tobacco CK2. Phosphopeptide mass mapping reveals that TGBp1 is phosphorylated in Ser-165, which is localized within a CK2 consensus sequence. Our results strongly suggest that a N. tabacum kinase of the CK2 family is involved in TBGp1 phosphorylation during the course of viral infection.
publishDate 2008
dc.date.none.fl_str_mv 2008-10
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/11336/79706
Modena, Natalia Andrea; Zelada, Alicia Mercedes; Conte, Ana Florencia; Mentaberry, Alejandro Nestor; Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity; Elsevier Science; Virus Research; 137; 1; 10-2008; 16-23
0168-1702
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79706
identifier_str_mv Modena, Natalia Andrea; Zelada, Alicia Mercedes; Conte, Ana Florencia; Mentaberry, Alejandro Nestor; Phosphorylation of the TGBp1 movement protein of Potato virus X by a Nicotiana tabacum CK2-like activity; Elsevier Science; Virus Research; 137; 1; 10-2008; 16-23
0168-1702
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/18632176
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.virusres.2008.04.007
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168170208001408
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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
_version_ 1842270062729232384
score 13.13397

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