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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/130681
Acceder
id CONICETDig_e5132277800d1606252e69d1a128a0d4
oai_identifier_str oai:ri.conicet.gov.ar:11336/130681
network_acronym_str CONICETDig
repository_id_str 3498
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
_version_ 1846083524945248256
score 13.22299

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