'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves

Massive degradation of photosynthetic proteins is the hallmark of leaf senescence; however the mechanism involved in chloroplast protein breakdown is not completely understood. As small 'senescence-associated vacuoles' (SAVs) with intense proteolytic activity accumulate in senescing leaves...

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Autores principales: Martínez, Dana Ethel, Costa, María Luján, Gomez, Facundo Martin, Otegui, Marisa, Guiamet, Juan José
Formato: Articulo
Lenguaje:Inglés
Publicado: 2008
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/84235
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id I19-R120-10915-84235
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Naturales
Chloroplast breakdown
Glutamine synthetase
Proteolysis
Rubisco
Senescence-associated vacuoles
Tobacco
spellingShingle Ciencias Naturales
Chloroplast breakdown
Glutamine synthetase
Proteolysis
Rubisco
Senescence-associated vacuoles
Tobacco
Martínez, Dana Ethel
Costa, María Luján
Gomez, Facundo Martin
Otegui, Marisa
Guiamet, Juan José
'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
topic_facet Ciencias Naturales
Chloroplast breakdown
Glutamine synthetase
Proteolysis
Rubisco
Senescence-associated vacuoles
Tobacco
description Massive degradation of photosynthetic proteins is the hallmark of leaf senescence; however the mechanism involved in chloroplast protein breakdown is not completely understood. As small 'senescence-associated vacuoles' (SAVs) with intense proteolytic activity accumulate in senescing leaves of soybean and Arabidopsis, the main goal of this work was to determine whether SAVs are involved in the degradation of chloroplastic components. SAVs with protease activity were readily detected through confocal microscopy of naturally senescing leaves of tobacco (<i>Nicotiana tabacum</i> L.). In detached leaves incubated in darkness, acceleration of the chloroplast degradation rate by ethylene treatment correlated with a twofold increase in the number of SAVs per cell, compared to untreated leaves. In a tobacco line expressing GFP targeted to plastids, GFP was re-located to SAVs in senescing leaves. SAVs were isolated by sucrose density gradient centrifugation. Isolated SAVs contained chloroplast-targeted GFP and the chloroplast stromal proteins Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) and glutamine synthetase, but lacked the thylakoid proteins D1 and light-harvesting complex II of the photosystem II reaction center and photosystem II antenna, respectively. In SAVs incubated at 30°C, there was a steady decrease in Rubisco levels, which was completely abolished by addition of protease inhibitors. These results indicate that SAVs are involved in degradation of the soluble photosynthetic proteins of the chloroplast stroma during senescence of leaves.
format Articulo
Articulo
author Martínez, Dana Ethel
Costa, María Luján
Gomez, Facundo Martin
Otegui, Marisa
Guiamet, Juan José
author_facet Martínez, Dana Ethel
Costa, María Luján
Gomez, Facundo Martin
Otegui, Marisa
Guiamet, Juan José
author_sort Martínez, Dana Ethel
title 'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
title_short 'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
title_full 'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
title_fullStr 'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
title_full_unstemmed 'Senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
title_sort 'senescence-associated vacuoles' are involved in the degradation of chloroplast proteins in tobacco leaves
publishDate 2008
url http://sedici.unlp.edu.ar/handle/10915/84235
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AT oteguimarisa senescenceassociatedvacuolesareinvolvedinthedegradationofchloroplastproteinsintobaccoleaves
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