Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72
- Autores
- Contreras Molina, Maria Isabel; Otegui, Marisa; Petruccelli, Silvana
- Año de publicación
- 2006
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Storage proteins are transported to a special storage compartments in seeds by Golgi dependent or independent pathways depending on the plant species. The aim of this work was to study the sunflower storage protein transport pathway and to identify component of the sorting machinery. Immature sunflower seeds were analyzed by subcellular fractionation (using percoll and sucrose gradients) and electron microscopy. The vesicles isolated with percoll, have precursors of 11S globulins, a-TIP, d-TIP, BiP, and two bands that have homology to the pumpkin vacuolar sorting receptor PV72. Sucrose isolated vesicles have the same composition than percoll ones, except for the lack of BiP and the presence of only one protein that has reactivity with pea VSR BP80. Electronic micrographies of developing seeds show that the formation of electron dense aggregates starts in the endoplasmic reticulum, and that these aggregates are very abundant in the trans-Golgi apparatus, where release of dense vesicles happens. These vesicles contain a homolog of PV72 in their membranes. Storage proteins are also detected in multivesicular bodies whose membranes have reactivity with PV72 serum. All these results indicated that sunflower storage proteins are transported to protein storage vacuoles by a Golgi dependent pathway in a process in which homologous of PV72 are involved.
Fil: Contreras Molina, Maria Isabel. Michigan State University; Estados Unidos
Fil: Otegui, Marisa. University of Wisconsin; Estados Unidos
Fil: Petruccelli, Silvana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina - Materia
-
Developing sunflower seeds
Storage proteins
Transport pathway
Vacuolar sorting
Vacuolar sorting receptor - 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:11336/115294
Ver los metadatos del registro completo
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network_name_str |
CONICET Digital (CONICET) |
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Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72Contreras Molina, Maria IsabelOtegui, MarisaPetruccelli, SilvanaDeveloping sunflower seedsStorage proteinsTransport pathwayVacuolar sortingVacuolar sorting receptorhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Storage proteins are transported to a special storage compartments in seeds by Golgi dependent or independent pathways depending on the plant species. The aim of this work was to study the sunflower storage protein transport pathway and to identify component of the sorting machinery. Immature sunflower seeds were analyzed by subcellular fractionation (using percoll and sucrose gradients) and electron microscopy. The vesicles isolated with percoll, have precursors of 11S globulins, a-TIP, d-TIP, BiP, and two bands that have homology to the pumpkin vacuolar sorting receptor PV72. Sucrose isolated vesicles have the same composition than percoll ones, except for the lack of BiP and the presence of only one protein that has reactivity with pea VSR BP80. Electronic micrographies of developing seeds show that the formation of electron dense aggregates starts in the endoplasmic reticulum, and that these aggregates are very abundant in the trans-Golgi apparatus, where release of dense vesicles happens. These vesicles contain a homolog of PV72 in their membranes. Storage proteins are also detected in multivesicular bodies whose membranes have reactivity with PV72 serum. All these results indicated that sunflower storage proteins are transported to protein storage vacuoles by a Golgi dependent pathway in a process in which homologous of PV72 are involved.Fil: Contreras Molina, Maria Isabel. Michigan State University; Estados UnidosFil: Otegui, Marisa. University of Wisconsin; Estados UnidosFil: Petruccelli, Silvana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaPontificia Universidad Católica de Valparaíso2006-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/115294Contreras Molina, Maria Isabel; Otegui, Marisa; Petruccelli, Silvana; Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 6-2006; 1-50717-3458CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://tinyurl.com/yyqqvxf5info:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue3-fulltext-21info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:01:52Zoai:ri.conicet.gov.ar:11336/115294instacron: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 10:01:52.939CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
title |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
spellingShingle |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 Contreras Molina, Maria Isabel Developing sunflower seeds Storage proteins Transport pathway Vacuolar sorting Vacuolar sorting receptor |
title_short |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
title_full |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
title_fullStr |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
title_full_unstemmed |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
title_sort |
Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72 |
dc.creator.none.fl_str_mv |
Contreras Molina, Maria Isabel Otegui, Marisa Petruccelli, Silvana |
author |
Contreras Molina, Maria Isabel |
author_facet |
Contreras Molina, Maria Isabel Otegui, Marisa Petruccelli, Silvana |
author_role |
author |
author2 |
Otegui, Marisa Petruccelli, Silvana |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Developing sunflower seeds Storage proteins Transport pathway Vacuolar sorting Vacuolar sorting receptor |
topic |
Developing sunflower seeds Storage proteins Transport pathway Vacuolar sorting Vacuolar sorting receptor |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Storage proteins are transported to a special storage compartments in seeds by Golgi dependent or independent pathways depending on the plant species. The aim of this work was to study the sunflower storage protein transport pathway and to identify component of the sorting machinery. Immature sunflower seeds were analyzed by subcellular fractionation (using percoll and sucrose gradients) and electron microscopy. The vesicles isolated with percoll, have precursors of 11S globulins, a-TIP, d-TIP, BiP, and two bands that have homology to the pumpkin vacuolar sorting receptor PV72. Sucrose isolated vesicles have the same composition than percoll ones, except for the lack of BiP and the presence of only one protein that has reactivity with pea VSR BP80. Electronic micrographies of developing seeds show that the formation of electron dense aggregates starts in the endoplasmic reticulum, and that these aggregates are very abundant in the trans-Golgi apparatus, where release of dense vesicles happens. These vesicles contain a homolog of PV72 in their membranes. Storage proteins are also detected in multivesicular bodies whose membranes have reactivity with PV72 serum. All these results indicated that sunflower storage proteins are transported to protein storage vacuoles by a Golgi dependent pathway in a process in which homologous of PV72 are involved. Fil: Contreras Molina, Maria Isabel. Michigan State University; Estados Unidos Fil: Otegui, Marisa. University of Wisconsin; Estados Unidos Fil: Petruccelli, Silvana. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina |
description |
Storage proteins are transported to a special storage compartments in seeds by Golgi dependent or independent pathways depending on the plant species. The aim of this work was to study the sunflower storage protein transport pathway and to identify component of the sorting machinery. Immature sunflower seeds were analyzed by subcellular fractionation (using percoll and sucrose gradients) and electron microscopy. The vesicles isolated with percoll, have precursors of 11S globulins, a-TIP, d-TIP, BiP, and two bands that have homology to the pumpkin vacuolar sorting receptor PV72. Sucrose isolated vesicles have the same composition than percoll ones, except for the lack of BiP and the presence of only one protein that has reactivity with pea VSR BP80. Electronic micrographies of developing seeds show that the formation of electron dense aggregates starts in the endoplasmic reticulum, and that these aggregates are very abundant in the trans-Golgi apparatus, where release of dense vesicles happens. These vesicles contain a homolog of PV72 in their membranes. Storage proteins are also detected in multivesicular bodies whose membranes have reactivity with PV72 serum. All these results indicated that sunflower storage proteins are transported to protein storage vacuoles by a Golgi dependent pathway in a process in which homologous of PV72 are involved. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-06 |
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/11336/115294 Contreras Molina, Maria Isabel; Otegui, Marisa; Petruccelli, Silvana; Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 6-2006; 1-5 0717-3458 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/115294 |
identifier_str_mv |
Contreras Molina, Maria Isabel; Otegui, Marisa; Petruccelli, Silvana; Sunflower storage proteins are transported in dense vesicles that contain proteins homologous to the pumpkin vacuolar sorting receptor PV 72; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 3; 6-2006; 1-5 0717-3458 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://tinyurl.com/yyqqvxf5 info:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue3-fulltext-21 |
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 |
Pontificia Universidad Católica de Valparaíso |
publisher.none.fl_str_mv |
Pontificia Universidad Católica de Valparaíso |
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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1844613817251659776 |
score |
13.070432 |