Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector
- Autores
- Wirthmueller, Lennart; Roth, Charlotte; Fabro, Georgina; Caillaud, Marie-Cécile; Rallapalli, Ghanasyam; Asai, Shuta; Sklenar, Jan; Jones, Alexandra M. E.; Wiermer, Marcel; Jones, Jonathan D. G.; Banfield, Mark J.
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells.
Fil: Wirthmueller, Lennart. John Innes Institute; Reino Unido. The Sainsbury Laboratory; Reino Unido
Fil: Roth, Charlotte. Georg‐August‐University; Alemania
Fil: Fabro, Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Caillaud, Marie-Cécile. The Sainsbury Laboratory; Reino Unido
Fil: Rallapalli, Ghanasyam. The Sainsbury Laboratory; Reino Unido
Fil: Asai, Shuta. The Sainsbury Laboratory; Reino Unido
Fil: Sklenar, Jan. John Innes Institute; Reino Unido
Fil: Jones, Alexandra M. E.. John Innes Institute; Reino Unido
Fil: Wiermer, Marcel. Georg‐August‐University; Alemania
Fil: Jones, Jonathan D. G.. The Sainsbury Laboratory; Reino Unido
Fil: Banfield, Mark J.. Georg‐August‐University; Alemania - Materia
-
ARABIDOPSIS THALIANA
HYALOPERONOSPORA ARABIDOPSIDIS
IMPORTIN-Α
NUCLEAR LOCALIZATION SEQUENCE
NUCLEO-CYTOPLASMIC TRANSPORT
OOMYCETE EFFECTOR
PLANT INNATE IMMUNITY - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/130681
Ver los metadatos del registro completo
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network_name_str |
CONICET Digital (CONICET) |
spelling |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effectorWirthmueller, LennartRoth, CharlotteFabro, GeorginaCaillaud, Marie-CécileRallapalli, GhanasyamAsai, ShutaSklenar, JanJones, Alexandra M. E.Wiermer, MarcelJones, Jonathan D. G.Banfield, Mark J.ARABIDOPSIS THALIANAHYALOPERONOSPORA ARABIDOPSIDISIMPORTIN-ΑNUCLEAR LOCALIZATION SEQUENCENUCLEO-CYTOPLASMIC TRANSPORTOOMYCETE EFFECTORPLANT INNATE IMMUNITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells.Fil: Wirthmueller, Lennart. John Innes Institute; Reino Unido. The Sainsbury Laboratory; Reino UnidoFil: Roth, Charlotte. Georg‐August‐University; AlemaniaFil: Fabro, Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Caillaud, Marie-Cécile. The Sainsbury Laboratory; Reino UnidoFil: Rallapalli, Ghanasyam. The Sainsbury Laboratory; Reino UnidoFil: Asai, Shuta. The Sainsbury Laboratory; Reino UnidoFil: Sklenar, Jan. John Innes Institute; Reino UnidoFil: Jones, Alexandra M. E.. John Innes Institute; Reino UnidoFil: Wiermer, Marcel. Georg‐August‐University; AlemaniaFil: Jones, Jonathan D. G.. The Sainsbury Laboratory; Reino UnidoFil: Banfield, Mark J.. Georg‐August‐University; AlemaniaWiley Blackwell Publishing, Inc2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/130681Wirthmueller, Lennart; Roth, Charlotte; Fabro, Georgina; Caillaud, Marie-Cécile; Rallapalli, Ghanasyam; et al.; Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector; Wiley Blackwell Publishing, Inc; Plant Journal; 81; 1; 1-2015; 40-520960-74121365-313XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/tpj.12691/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1111/tpj.12691info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:41:24Zoai:ri.conicet.gov.ar:11336/130681instacron: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:34982025-10-15 15:41:25.054CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
title |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
spellingShingle |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector Wirthmueller, Lennart ARABIDOPSIS THALIANA HYALOPERONOSPORA ARABIDOPSIDIS IMPORTIN-Α NUCLEAR LOCALIZATION SEQUENCE NUCLEO-CYTOPLASMIC TRANSPORT OOMYCETE EFFECTOR PLANT INNATE IMMUNITY |
title_short |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
title_full |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
title_fullStr |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
title_full_unstemmed |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
title_sort |
Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector |
dc.creator.none.fl_str_mv |
Wirthmueller, Lennart Roth, Charlotte Fabro, Georgina Caillaud, Marie-Cécile Rallapalli, Ghanasyam Asai, Shuta Sklenar, Jan Jones, Alexandra M. E. Wiermer, Marcel Jones, Jonathan D. G. Banfield, Mark J. |
author |
Wirthmueller, Lennart |
author_facet |
Wirthmueller, Lennart Roth, Charlotte Fabro, Georgina Caillaud, Marie-Cécile Rallapalli, Ghanasyam Asai, Shuta Sklenar, Jan Jones, Alexandra M. E. Wiermer, Marcel Jones, Jonathan D. G. Banfield, Mark J. |
author_role |
author |
author2 |
Roth, Charlotte Fabro, Georgina Caillaud, Marie-Cécile Rallapalli, Ghanasyam Asai, Shuta Sklenar, Jan Jones, Alexandra M. E. Wiermer, Marcel Jones, Jonathan D. G. Banfield, Mark J. |
author2_role |
author author author author author author author author author author |
dc.subject.none.fl_str_mv |
ARABIDOPSIS THALIANA HYALOPERONOSPORA ARABIDOPSIDIS IMPORTIN-Α NUCLEAR LOCALIZATION SEQUENCE NUCLEO-CYTOPLASMIC TRANSPORT OOMYCETE EFFECTOR PLANT INNATE IMMUNITY |
topic |
ARABIDOPSIS THALIANA HYALOPERONOSPORA ARABIDOPSIDIS IMPORTIN-Α NUCLEAR LOCALIZATION SEQUENCE NUCLEO-CYTOPLASMIC TRANSPORT OOMYCETE EFFECTOR PLANT INNATE IMMUNITY |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells. Fil: Wirthmueller, Lennart. John Innes Institute; Reino Unido. The Sainsbury Laboratory; Reino Unido Fil: Roth, Charlotte. Georg‐August‐University; Alemania Fil: Fabro, Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Caillaud, Marie-Cécile. The Sainsbury Laboratory; Reino Unido Fil: Rallapalli, Ghanasyam. The Sainsbury Laboratory; Reino Unido Fil: Asai, Shuta. The Sainsbury Laboratory; Reino Unido Fil: Sklenar, Jan. John Innes Institute; Reino Unido Fil: Jones, Alexandra M. E.. John Innes Institute; Reino Unido Fil: Wiermer, Marcel. Georg‐August‐University; Alemania Fil: Jones, Jonathan D. G.. The Sainsbury Laboratory; Reino Unido Fil: Banfield, Mark J.. Georg‐August‐University; Alemania |
description |
Importin-αs are essential adapter proteins that recruit cytoplasmic proteins destined for active nuclear import to the nuclear transport machinery. Cargo proteins interact with the importin-α armadillo repeat domain via nuclear localization sequences (NLSs), short amino acids motifs enriched in Lys and Arg residues. Plant genomes typically encode several importin-α paralogs that can have both specific and partially redundant functions. Although some cargos are preferentially imported by a distinct importin-α it remains unknown how this specificity is generated and to what extent cargos compete for binding to nuclear transport receptors. Here we report that the effector protein HaRxL106 from the oomycete pathogen Hyaloperonospora arabidopsidis co-opts the host cell's nuclear import machinery. We use HaRxL106 as a probe to determine redundant and specific functions of importin-α paralogs from Arabidopsis thaliana. A crystal structure of the importin-α3/MOS6 armadillo repeat domain suggests that five of the six Arabidopsis importin-αs expressed in rosette leaves have an almost identical NLS-binding site. Comparison of the importin-α binding affinities of HaRxL106 and other cargos in vitro and in plant cells suggests that relatively small affinity differences in vitro affect the rate of transport complex formation in vivo. Our results suggest that cargo affinity for importin-α, sequence variation at the importin-α NLS-binding sites and tissue-specific expression levels of importin-αs determine formation of cargo/importin-α transport complexes in plant cells. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-01 |
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/11336/130681 Wirthmueller, Lennart; Roth, Charlotte; Fabro, Georgina; Caillaud, Marie-Cécile; Rallapalli, Ghanasyam; et al.; Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector; Wiley Blackwell Publishing, Inc; Plant Journal; 81; 1; 1-2015; 40-52 0960-7412 1365-313X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/130681 |
identifier_str_mv |
Wirthmueller, Lennart; Roth, Charlotte; Fabro, Georgina; Caillaud, Marie-Cécile; Rallapalli, Ghanasyam; et al.; Probing formation of cargo/importin-α transport complexes in plant cells using a pathogen effector; Wiley Blackwell Publishing, Inc; Plant Journal; 81; 1; 1-2015; 40-52 0960-7412 1365-313X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/tpj.12691/abstract info:eu-repo/semantics/altIdentifier/doi/10.1111/tpj.12691 |
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 |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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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1846083524945248256 |
score |
13.22299 |