The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness

Autores
Roberts, Irma; Fernandez Murray, Jorge Pedro; Passeron, Susana; Barneix, Atilio José
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In the present paper, we studied the participation of the 20S proteasome, the proteolytic component of the ubiquitin-proteasome pathway, in the remobilization of bulk proteins in senescing wheat leaves. The detached leaves of 15-d-old plants were incubated in darkness for several days, and various proteolytic activities were analysed in soluble extracts prepared at 0, 48 and 96 h after detachment. The endoproteolytic activity, measured at pH 7.5 and 5.4, increased more than 10-fold and the total peptidasic activity increased up to 5-fold after 96 h of incubation in the dark, when expressed as specific activity. In the same period, the leaf-protein content decreased to less than 50% of that present at the initial time. The 20S proteasome chymotrypsin-like activity remained constant when it was expressed as activity per leaf fresh weight and resulted 2-fold higher in terms of specific activity. The western blot analysis showed that the amount of 20S proteasome protein and ubiquitin-protein conjugates also remained constant until 4 d of incubation in darkness. These results indicate that the ubiquitin-proteasome pathway remains functional until the late phases of senescence suggesting that it may participate in the regulatory aspects of the process rather than in the massive protein breakdown.
Fil: Roberts, Irma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Fernandez Murray, Jorge Pedro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Passeron, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Barneix, Atilio José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Materia
20S PROTEASOME
PROTEOLYSIS
SENESCENCE
UBIQUITIN
WHEAT
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:11336/148958

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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darknessRoberts, IrmaFernandez Murray, Jorge PedroPasseron, SusanaBarneix, Atilio José20S PROTEASOMEPROTEOLYSISSENESCENCEUBIQUITINWHEAThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In the present paper, we studied the participation of the 20S proteasome, the proteolytic component of the ubiquitin-proteasome pathway, in the remobilization of bulk proteins in senescing wheat leaves. The detached leaves of 15-d-old plants were incubated in darkness for several days, and various proteolytic activities were analysed in soluble extracts prepared at 0, 48 and 96 h after detachment. The endoproteolytic activity, measured at pH 7.5 and 5.4, increased more than 10-fold and the total peptidasic activity increased up to 5-fold after 96 h of incubation in the dark, when expressed as specific activity. In the same period, the leaf-protein content decreased to less than 50% of that present at the initial time. The 20S proteasome chymotrypsin-like activity remained constant when it was expressed as activity per leaf fresh weight and resulted 2-fold higher in terms of specific activity. The western blot analysis showed that the amount of 20S proteasome protein and ubiquitin-protein conjugates also remained constant until 4 d of incubation in darkness. These results indicate that the ubiquitin-proteasome pathway remains functional until the late phases of senescence suggesting that it may participate in the regulatory aspects of the process rather than in the massive protein breakdown.Fil: Roberts, Irma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; ArgentinaFil: Fernandez Murray, Jorge Pedro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; ArgentinaFil: Passeron, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; ArgentinaFil: Barneix, Atilio José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; ArgentinaElsevier France-Editions Scientifiques Medicales Elsevier2002-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/148958Roberts, Irma; Fernandez Murray, Jorge Pedro; Passeron, Susana; Barneix, Atilio José; The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness; Elsevier France-Editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 40; 2; 2-2002; 161-1660981-94281873-2690CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0981942801013493info:eu-repo/semantics/altIdentifier/doi/10.1016/s0981-9428(01)01349-3info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:31:12Zoai:ri.conicet.gov.ar:11336/148958instacron: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 10:31:13.14CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
title The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
spellingShingle The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
Roberts, Irma
20S PROTEASOME
PROTEOLYSIS
SENESCENCE
UBIQUITIN
WHEAT
title_short The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
title_full The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
title_fullStr The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
title_full_unstemmed The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
title_sort The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness
dc.creator.none.fl_str_mv Roberts, Irma
Fernandez Murray, Jorge Pedro
Passeron, Susana
Barneix, Atilio José
author Roberts, Irma
author_facet Roberts, Irma
Fernandez Murray, Jorge Pedro
Passeron, Susana
Barneix, Atilio José
author_role author
author2 Fernandez Murray, Jorge Pedro
Passeron, Susana
Barneix, Atilio José
author2_role author
author
author
dc.subject.none.fl_str_mv 20S PROTEASOME
PROTEOLYSIS
SENESCENCE
UBIQUITIN
WHEAT
topic 20S PROTEASOME
PROTEOLYSIS
SENESCENCE
UBIQUITIN
WHEAT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In the present paper, we studied the participation of the 20S proteasome, the proteolytic component of the ubiquitin-proteasome pathway, in the remobilization of bulk proteins in senescing wheat leaves. The detached leaves of 15-d-old plants were incubated in darkness for several days, and various proteolytic activities were analysed in soluble extracts prepared at 0, 48 and 96 h after detachment. The endoproteolytic activity, measured at pH 7.5 and 5.4, increased more than 10-fold and the total peptidasic activity increased up to 5-fold after 96 h of incubation in the dark, when expressed as specific activity. In the same period, the leaf-protein content decreased to less than 50% of that present at the initial time. The 20S proteasome chymotrypsin-like activity remained constant when it was expressed as activity per leaf fresh weight and resulted 2-fold higher in terms of specific activity. The western blot analysis showed that the amount of 20S proteasome protein and ubiquitin-protein conjugates also remained constant until 4 d of incubation in darkness. These results indicate that the ubiquitin-proteasome pathway remains functional until the late phases of senescence suggesting that it may participate in the regulatory aspects of the process rather than in the massive protein breakdown.
Fil: Roberts, Irma. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Fernandez Murray, Jorge Pedro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Passeron, Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
Fil: Barneix, Atilio José. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales. Universidad de Buenos Aires. Facultad de Agronomía. Instituto de Investigaciones en Biociencias Agrícolas y Ambientales; Argentina
description In the present paper, we studied the participation of the 20S proteasome, the proteolytic component of the ubiquitin-proteasome pathway, in the remobilization of bulk proteins in senescing wheat leaves. The detached leaves of 15-d-old plants were incubated in darkness for several days, and various proteolytic activities were analysed in soluble extracts prepared at 0, 48 and 96 h after detachment. The endoproteolytic activity, measured at pH 7.5 and 5.4, increased more than 10-fold and the total peptidasic activity increased up to 5-fold after 96 h of incubation in the dark, when expressed as specific activity. In the same period, the leaf-protein content decreased to less than 50% of that present at the initial time. The 20S proteasome chymotrypsin-like activity remained constant when it was expressed as activity per leaf fresh weight and resulted 2-fold higher in terms of specific activity. The western blot analysis showed that the amount of 20S proteasome protein and ubiquitin-protein conjugates also remained constant until 4 d of incubation in darkness. These results indicate that the ubiquitin-proteasome pathway remains functional until the late phases of senescence suggesting that it may participate in the regulatory aspects of the process rather than in the massive protein breakdown.
publishDate 2002
dc.date.none.fl_str_mv 2002-02
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/11336/148958
Roberts, Irma; Fernandez Murray, Jorge Pedro; Passeron, Susana; Barneix, Atilio José; The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness; Elsevier France-Editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 40; 2; 2-2002; 161-166
0981-9428
1873-2690
CONICET Digital
CONICET
url http://hdl.handle.net/11336/148958
identifier_str_mv Roberts, Irma; Fernandez Murray, Jorge Pedro; Passeron, Susana; Barneix, Atilio José; The activity of the 20S proteasome is maintained in detached wheat leaves during senescence in darkness; Elsevier France-Editions Scientifiques Medicales Elsevier; Plant Physiology and Biochemistry; 40; 2; 2-2002; 161-166
0981-9428
1873-2690
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.sciencedirect.com/science/article/pii/S0981942801013493
info:eu-repo/semantics/altIdentifier/doi/10.1016/s0981-9428(01)01349-3
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 Elsevier France-Editions Scientifiques Medicales Elsevier
publisher.none.fl_str_mv Elsevier France-Editions Scientifiques Medicales Elsevier
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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