Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity

Autores
Danna, Cristian H.; Bartoli, Carlos Guillermo; Sacco, Francisco; Ingala, Lorena R.; Santa María, Guillermo E.; Guiamet, Juan José; Ugalde, Rodolfo A.
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In chloroplasts, stromal and thylakoid-bound ascorbate peroxidases (tAPX) play a major role in the removal of H2O2 produced during photosynthesis. Here, we report that hexaploid wheat (Triticum aestivum) expresses three homeologous tAPX genes (TaAPX-6A, TaAPX-6B, and TaAPX-6D) mapping on group-6 chromosomes. The tAPX activity of a mutant line lacking TaAPX-6B was 40% lower than that of the wild type. When grown at high-light intensity photosystem II electron transfer, photosynthetic activity and biomass accumulation were significantly reduced in this mutant, suggesting that tAPX activity is essential for photosynthesis. Despite the reduced tAPX activity, mutant plants did not exhibit oxidative damage probably due to the reduced photochemical activity. This might be the result of a compensating mechanism to prevent oxidative damage having as a consequence a decrease in growth of the tAPX mutant plants.
Instituto de Fisiología Vegetal
Facultad de Ciencias Agrarias y Forestales
Materia
Ciencias Agrarias
Ciencias Exactas
ascorbate
H2O2
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/84571
Acceder
id SEDICI_044c15a1e8432b012b5f187f78a3371c
oai_identifier_str oai:sedici.unlp.edu.ar:10915/84571
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activityDanna, Cristian H.Bartoli, Carlos GuillermoSacco, FranciscoIngala, Lorena R.Santa María, Guillermo E.Guiamet, Juan JoséUgalde, Rodolfo A.Ciencias AgrariasCiencias ExactasascorbateH2O2In chloroplasts, stromal and thylakoid-bound ascorbate peroxidases (tAPX) play a major role in the removal of H<SUB>2</SUB>O<SUB>2</SUB> produced during photosynthesis. Here, we report that hexaploid wheat (<i>Triticum aestivum</i>) expresses three homeologous tAPX genes (TaAPX-6A, TaAPX-6B, and TaAPX-6D) mapping on group-6 chromosomes. The tAPX activity of a mutant line lacking TaAPX-6B was 40% lower than that of the wild type. When grown at high-light intensity photosystem II electron transfer, photosynthetic activity and biomass accumulation were significantly reduced in this mutant, suggesting that tAPX activity is essential for photosynthesis. Despite the reduced tAPX activity, mutant plants did not exhibit oxidative damage probably due to the reduced photochemical activity. This might be the result of a compensating mechanism to prevent oxidative damage having as a consequence a decrease in growth of the tAPX mutant plants.Instituto de Fisiología VegetalFacultad de Ciencias Agrarias y Forestales2003info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf2116-2125http://sedici.unlp.edu.ar/handle/10915/84571enginfo:eu-repo/semantics/altIdentifier/issn/0032-0889info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.103.021717info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:15Zoai:sedici.unlp.edu.ar:10915/84571Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:16.096SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
title Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
spellingShingle Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
Danna, Cristian H.
Ciencias Agrarias
Ciencias Exactas
ascorbate
H2O2
title_short Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
title_full Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
title_fullStr Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
title_full_unstemmed Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
title_sort Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
dc.creator.none.fl_str_mv Danna, Cristian H.
Bartoli, Carlos Guillermo
Sacco, Francisco
Ingala, Lorena R.
Santa María, Guillermo E.
Guiamet, Juan José
Ugalde, Rodolfo A.
author Danna, Cristian H.
author_facet Danna, Cristian H.
Bartoli, Carlos Guillermo
Sacco, Francisco
Ingala, Lorena R.
Santa María, Guillermo E.
Guiamet, Juan José
Ugalde, Rodolfo A.
author_role author
author2 Bartoli, Carlos Guillermo
Sacco, Francisco
Ingala, Lorena R.
Santa María, Guillermo E.
Guiamet, Juan José
Ugalde, Rodolfo A.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Agrarias
Ciencias Exactas
ascorbate
H2O2
topic Ciencias Agrarias
Ciencias Exactas
ascorbate
H2O2
dc.description.none.fl_txt_mv In chloroplasts, stromal and thylakoid-bound ascorbate peroxidases (tAPX) play a major role in the removal of H<SUB>2</SUB>O<SUB>2</SUB> produced during photosynthesis. Here, we report that hexaploid wheat (<i>Triticum aestivum</i>) expresses three homeologous tAPX genes (TaAPX-6A, TaAPX-6B, and TaAPX-6D) mapping on group-6 chromosomes. The tAPX activity of a mutant line lacking TaAPX-6B was 40% lower than that of the wild type. When grown at high-light intensity photosystem II electron transfer, photosynthetic activity and biomass accumulation were significantly reduced in this mutant, suggesting that tAPX activity is essential for photosynthesis. Despite the reduced tAPX activity, mutant plants did not exhibit oxidative damage probably due to the reduced photochemical activity. This might be the result of a compensating mechanism to prevent oxidative damage having as a consequence a decrease in growth of the tAPX mutant plants.
Instituto de Fisiología Vegetal
Facultad de Ciencias Agrarias y Forestales
description In chloroplasts, stromal and thylakoid-bound ascorbate peroxidases (tAPX) play a major role in the removal of H<SUB>2</SUB>O<SUB>2</SUB> produced during photosynthesis. Here, we report that hexaploid wheat (<i>Triticum aestivum</i>) expresses three homeologous tAPX genes (TaAPX-6A, TaAPX-6B, and TaAPX-6D) mapping on group-6 chromosomes. The tAPX activity of a mutant line lacking TaAPX-6B was 40% lower than that of the wild type. When grown at high-light intensity photosystem II electron transfer, photosynthetic activity and biomass accumulation were significantly reduced in this mutant, suggesting that tAPX activity is essential for photosynthesis. Despite the reduced tAPX activity, mutant plants did not exhibit oxidative damage probably due to the reduced photochemical activity. This might be the result of a compensating mechanism to prevent oxidative damage having as a consequence a decrease in growth of the tAPX mutant plants.
publishDate 2003
dc.date.none.fl_str_mv 2003
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/84571
url http://sedici.unlp.edu.ar/handle/10915/84571
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0032-0889
info:eu-repo/semantics/altIdentifier/doi/10.1104/pp.103.021717
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
2116-2125
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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