Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism

Autores
Lescano López, Ignacio; Bogino, María Florencia; Martini, Ana Carolina; Tessi, Tomás María; González, Claudio Alejandro; Schumacher, Karin; Desimone, Marcelo
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Allantoin is a purine oxidative product involved in long distance transport of organic nitrogen in nodulating legumes and was recently shown to play a role in stress tolerance in other plants. The subcellular localization of enzymes that catalyze allantoin synthesis and degradation indicates that allantoin is produced in peroxisomes and degraded in the endoplasmic reticulum (ER). Although it has been determined that allantoin is mostly synthesized in roots and transported to shoots either for organic nitrogen translocation in legumes or for plant protection during stress in Arabidopsis (Arabidopsis thaliana), the mechanism and molecular components of allantoin export from root cells are still unknown. AtUPS5 (Arabidopsis UREIDE PERMEASE 5) is a transmembrane protein that transports allantoin with high affinity when expressed in yeast. The subcellular fate of splicing variants AtUPS5L (long) and AtUPS5S (short) was studied by tagging them with fluorescent proteins in their cytosolic loops. The capability of these fusion proteins to complement the function of the native proteins was demonstrated by nutritional and salt stress experiments. Both variants localized to the ER, but the AtUPS5L variant was also detected in the trans-Golgi network/early endosome and at the plasma membrane. AtUPS5L and AtUPS5S localization indicates that they could have different roles in allantoin distribution between subcellular compartments. Our data suggest that under nonstress conditions UPS5L and UPS5S may function in allantoin degradation for nutrient recycling, whereas under stress, both genes may be involved in vesicular export allowing allantoin translocation from roots to shoots.
Fil: Lescano López, Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. 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: Bogino, María Florencia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina
Fil: Martini, Ana Carolina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Tessi, Tomás María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: González, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina
Fil: Schumacher, Karin. Heidelberg University. Centre For Organismal Studies; Alemania
Fil: Desimone, Marcelo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Materia
ALLANTOIN
SECRETORY PATHWAY
ARABIDOPSIS
TRANSPORT
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:11336/128871
Acceder
id CONICETDig_3d983d5db2f8bf047590ab10656f3f90
oai_identifier_str oai:ri.conicet.gov.ar:11336/128871
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolismLescano López, IgnacioBogino, María FlorenciaMartini, Ana CarolinaTessi, Tomás MaríaGonzález, Claudio AlejandroSchumacher, KarinDesimone, MarceloALLANTOINSECRETORY PATHWAYARABIDOPSISTRANSPORThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Allantoin is a purine oxidative product involved in long distance transport of organic nitrogen in nodulating legumes and was recently shown to play a role in stress tolerance in other plants. The subcellular localization of enzymes that catalyze allantoin synthesis and degradation indicates that allantoin is produced in peroxisomes and degraded in the endoplasmic reticulum (ER). Although it has been determined that allantoin is mostly synthesized in roots and transported to shoots either for organic nitrogen translocation in legumes or for plant protection during stress in Arabidopsis (Arabidopsis thaliana), the mechanism and molecular components of allantoin export from root cells are still unknown. AtUPS5 (Arabidopsis UREIDE PERMEASE 5) is a transmembrane protein that transports allantoin with high affinity when expressed in yeast. The subcellular fate of splicing variants AtUPS5L (long) and AtUPS5S (short) was studied by tagging them with fluorescent proteins in their cytosolic loops. The capability of these fusion proteins to complement the function of the native proteins was demonstrated by nutritional and salt stress experiments. Both variants localized to the ER, but the AtUPS5L variant was also detected in the trans-Golgi network/early endosome and at the plasma membrane. AtUPS5L and AtUPS5S localization indicates that they could have different roles in allantoin distribution between subcellular compartments. Our data suggest that under nonstress conditions UPS5L and UPS5S may function in allantoin degradation for nutrient recycling, whereas under stress, both genes may be involved in vesicular export allowing allantoin translocation from roots to shoots.Fil: Lescano López, Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. 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: Bogino, María Florencia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; ArgentinaFil: Martini, Ana Carolina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; ArgentinaFil: Tessi, Tomás María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaFil: González, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; ArgentinaFil: Schumacher, Karin. Heidelberg University. Centre For Organismal Studies; AlemaniaFil: Desimone, Marcelo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; ArgentinaAmerican Society of Plant Biologist2019-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/128871Lescano López, Ignacio; Bogino, María Florencia; Martini, Ana Carolina; Tessi, Tomás María; González, Claudio Alejandro; et al.; Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism; American Society of Plant Biologist; Plant Physiology; 182; 3; 12-2019; 1310-13250032-08891532-2548CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.plantphysiol.org/content/early/2019/12/20/pp.19.01136info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.19.01136info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/plphys/article/182/3/1310/6116261info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:02Zoai:ri.conicet.gov.ar:11336/128871instacron: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:34982025-09-29 10:01:02.794CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
title Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
spellingShingle Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
Lescano López, Ignacio
ALLANTOIN
SECRETORY PATHWAY
ARABIDOPSIS
TRANSPORT
title_short Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
title_full Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
title_fullStr Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
title_full_unstemmed Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
title_sort Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism
dc.creator.none.fl_str_mv Lescano López, Ignacio
Bogino, María Florencia
Martini, Ana Carolina
Tessi, Tomás María
González, Claudio Alejandro
Schumacher, Karin
Desimone, Marcelo
author Lescano López, Ignacio
author_facet Lescano López, Ignacio
Bogino, María Florencia
Martini, Ana Carolina
Tessi, Tomás María
González, Claudio Alejandro
Schumacher, Karin
Desimone, Marcelo
author_role author
author2 Bogino, María Florencia
Martini, Ana Carolina
Tessi, Tomás María
González, Claudio Alejandro
Schumacher, Karin
Desimone, Marcelo
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ALLANTOIN
SECRETORY PATHWAY
ARABIDOPSIS
TRANSPORT
topic ALLANTOIN
SECRETORY PATHWAY
ARABIDOPSIS
TRANSPORT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Allantoin is a purine oxidative product involved in long distance transport of organic nitrogen in nodulating legumes and was recently shown to play a role in stress tolerance in other plants. The subcellular localization of enzymes that catalyze allantoin synthesis and degradation indicates that allantoin is produced in peroxisomes and degraded in the endoplasmic reticulum (ER). Although it has been determined that allantoin is mostly synthesized in roots and transported to shoots either for organic nitrogen translocation in legumes or for plant protection during stress in Arabidopsis (Arabidopsis thaliana), the mechanism and molecular components of allantoin export from root cells are still unknown. AtUPS5 (Arabidopsis UREIDE PERMEASE 5) is a transmembrane protein that transports allantoin with high affinity when expressed in yeast. The subcellular fate of splicing variants AtUPS5L (long) and AtUPS5S (short) was studied by tagging them with fluorescent proteins in their cytosolic loops. The capability of these fusion proteins to complement the function of the native proteins was demonstrated by nutritional and salt stress experiments. Both variants localized to the ER, but the AtUPS5L variant was also detected in the trans-Golgi network/early endosome and at the plasma membrane. AtUPS5L and AtUPS5S localization indicates that they could have different roles in allantoin distribution between subcellular compartments. Our data suggest that under nonstress conditions UPS5L and UPS5S may function in allantoin degradation for nutrient recycling, whereas under stress, both genes may be involved in vesicular export allowing allantoin translocation from roots to shoots.
Fil: Lescano López, Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. 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: Bogino, María Florencia. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina
Fil: Martini, Ana Carolina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Ciencias de la Salud. Universidad Nacional de Córdoba. Instituto de Investigaciones en Ciencias de la Salud; Argentina
Fil: Tessi, Tomás María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
Fil: González, Claudio Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina
Fil: Schumacher, Karin. Heidelberg University. Centre For Organismal Studies; Alemania
Fil: Desimone, Marcelo. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Departamento de Fisiología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina
description Allantoin is a purine oxidative product involved in long distance transport of organic nitrogen in nodulating legumes and was recently shown to play a role in stress tolerance in other plants. The subcellular localization of enzymes that catalyze allantoin synthesis and degradation indicates that allantoin is produced in peroxisomes and degraded in the endoplasmic reticulum (ER). Although it has been determined that allantoin is mostly synthesized in roots and transported to shoots either for organic nitrogen translocation in legumes or for plant protection during stress in Arabidopsis (Arabidopsis thaliana), the mechanism and molecular components of allantoin export from root cells are still unknown. AtUPS5 (Arabidopsis UREIDE PERMEASE 5) is a transmembrane protein that transports allantoin with high affinity when expressed in yeast. The subcellular fate of splicing variants AtUPS5L (long) and AtUPS5S (short) was studied by tagging them with fluorescent proteins in their cytosolic loops. The capability of these fusion proteins to complement the function of the native proteins was demonstrated by nutritional and salt stress experiments. Both variants localized to the ER, but the AtUPS5L variant was also detected in the trans-Golgi network/early endosome and at the plasma membrane. AtUPS5L and AtUPS5S localization indicates that they could have different roles in allantoin distribution between subcellular compartments. Our data suggest that under nonstress conditions UPS5L and UPS5S may function in allantoin degradation for nutrient recycling, whereas under stress, both genes may be involved in vesicular export allowing allantoin translocation from roots to shoots.
publishDate 2019
dc.date.none.fl_str_mv 2019-12
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/11336/128871
Lescano López, Ignacio; Bogino, María Florencia; Martini, Ana Carolina; Tessi, Tomás María; González, Claudio Alejandro; et al.; Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism; American Society of Plant Biologist; Plant Physiology; 182; 3; 12-2019; 1310-1325
0032-0889
1532-2548
CONICET Digital
CONICET
url http://hdl.handle.net/11336/128871
identifier_str_mv Lescano López, Ignacio; Bogino, María Florencia; Martini, Ana Carolina; Tessi, Tomás María; González, Claudio Alejandro; et al.; Ureide permease 5 (AtUPS5) connects cell compartments involved in UREIDE metabolism; American Society of Plant Biologist; Plant Physiology; 182; 3; 12-2019; 1310-1325
0032-0889
1532-2548
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://www.plantphysiol.org/content/early/2019/12/20/pp.19.01136
info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.19.01136
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/plphys/article/182/3/1310/6116261
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 American Society of Plant Biologist
publisher.none.fl_str_mv American Society of Plant Biologist
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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score 13.070432

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