Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation

Autores
Soto, Gabriela Cynthia; Stritzler, Margarita; Lisi, Christian Daniel; Alleva, Karina Edith; Pagano, María Elba; Ardila, Fernando; Mozzicafreddo, Matteo; Cuccioloni, Massimiliano; Angeletti, Mauro; Ayub, Nicolás Daniel
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Acetoacetyl-CoA thiolase (EC 2.3.1.9), also called thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA. This is the first enzymatic step in the biosynthesis of isoprenoids via mevalonate (MVA). In this work, thiolase II from alfalfa (MsAACT1) was identified and cloned. The enzymatic activity was experimentally demonstrated in planta and in heterologous systems. The condensation reaction by MsAACT1 was proved to be inhibited by CoA suggesting a negative feedback regulation of isoprenoid production. Real-time RT-PCR analysis indicated that MsAACT1 expression is highly increased in roots and leaves under cold and salinity stress. Treatment with mevastatin, a specific inhibitor of the MVA pathway, resulted in a decrease in squalene production, antioxidant activity, and the survival of stressed plants. As expected, the presence of mevastatin did not change chlorophyll and carotenoid levels, isoprenoids synthesized via the plastidial MVA-independent pathway. The addition of vitamin C suppressed the sensitive phenotype of plants challenged with mevastatin, suggesting a critical function of the MVA pathway in abiotic stress-inducible antioxidant defence. MsAACT1 over-expressing transgenic plants showed salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without altering the 3-hydroxy-3-methylglutaryl- CoA reductase (HMGR) activity in salt-stress conditions. Thus, acetoacetyl-CoA thiolase is a regulatory enzyme in isoprenoid biosynthesis involved in abiotic stress adaptation.
Fil: Soto, Gabriela Cynthia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Stritzler, Margarita. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lisi, Christian Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
Fil: Pagano, María Elba. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Ardila, Fernando. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Mozzicafreddo, Matteo. Universita Degli Di Camerino; Italia
Fil: Cuccioloni, Massimiliano. Universita Degli Di Camerino; Italia
Fil: Angeletti, Mauro. Universita Degli Di Camerino; Italia
Fil: Ayub, Nicolás Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Materia
ABIOTIC STRESS
ACETOACETYL-COA THIOLASE
ISOPRENOID
MVA PATHWAY
THIOLASE II
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:11336/114222
Acceder
id CONICETDig_bfb1dda95dd6da571206b4252647e1e8
oai_identifier_str oai:ri.conicet.gov.ar:11336/114222
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptationSoto, Gabriela CynthiaStritzler, MargaritaLisi, Christian DanielAlleva, Karina EdithPagano, María ElbaArdila, FernandoMozzicafreddo, MatteoCuccioloni, MassimilianoAngeletti, MauroAyub, Nicolás DanielABIOTIC STRESSACETOACETYL-COA THIOLASEISOPRENOIDMVA PATHWAYTHIOLASE IIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Acetoacetyl-CoA thiolase (EC 2.3.1.9), also called thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA. This is the first enzymatic step in the biosynthesis of isoprenoids via mevalonate (MVA). In this work, thiolase II from alfalfa (MsAACT1) was identified and cloned. The enzymatic activity was experimentally demonstrated in planta and in heterologous systems. The condensation reaction by MsAACT1 was proved to be inhibited by CoA suggesting a negative feedback regulation of isoprenoid production. Real-time RT-PCR analysis indicated that MsAACT1 expression is highly increased in roots and leaves under cold and salinity stress. Treatment with mevastatin, a specific inhibitor of the MVA pathway, resulted in a decrease in squalene production, antioxidant activity, and the survival of stressed plants. As expected, the presence of mevastatin did not change chlorophyll and carotenoid levels, isoprenoids synthesized via the plastidial MVA-independent pathway. The addition of vitamin C suppressed the sensitive phenotype of plants challenged with mevastatin, suggesting a critical function of the MVA pathway in abiotic stress-inducible antioxidant defence. MsAACT1 over-expressing transgenic plants showed salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without altering the 3-hydroxy-3-methylglutaryl- CoA reductase (HMGR) activity in salt-stress conditions. Thus, acetoacetyl-CoA thiolase is a regulatory enzyme in isoprenoid biosynthesis involved in abiotic stress adaptation.Fil: Soto, Gabriela Cynthia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; ArgentinaFil: Stritzler, Margarita. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lisi, Christian Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; ArgentinaFil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; ArgentinaFil: Pagano, María Elba. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; ArgentinaFil: Ardila, Fernando. Instituto Nacional de Tecnología Agropecuaria; ArgentinaFil: Mozzicafreddo, Matteo. Universita Degli Di Camerino; ItaliaFil: Cuccioloni, Massimiliano. Universita Degli Di Camerino; ItaliaFil: Angeletti, Mauro. Universita Degli Di Camerino; ItaliaFil: Ayub, Nicolás Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; ArgentinaOxford University Press2011-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/114222Soto, Gabriela Cynthia; Stritzler, Margarita; Lisi, Christian Daniel; Alleva, Karina Edith; Pagano, María Elba; et al.; Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation; Oxford University Press; Journal of Experimental Botany; 62; 15; 11-2011; 5699-57110022-0957CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jxb/article/62/15/5699/563304info:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/err287info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:06:29Zoai:ri.conicet.gov.ar:11336/114222instacron: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:34982025-09-10 13:06:30.284CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
title Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
spellingShingle Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
Soto, Gabriela Cynthia
ABIOTIC STRESS
ACETOACETYL-COA THIOLASE
ISOPRENOID
MVA PATHWAY
THIOLASE II
title_short Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
title_full Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
title_fullStr Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
title_full_unstemmed Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
title_sort Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation
dc.creator.none.fl_str_mv Soto, Gabriela Cynthia
Stritzler, Margarita
Lisi, Christian Daniel
Alleva, Karina Edith
Pagano, María Elba
Ardila, Fernando
Mozzicafreddo, Matteo
Cuccioloni, Massimiliano
Angeletti, Mauro
Ayub, Nicolás Daniel
author Soto, Gabriela Cynthia
author_facet Soto, Gabriela Cynthia
Stritzler, Margarita
Lisi, Christian Daniel
Alleva, Karina Edith
Pagano, María Elba
Ardila, Fernando
Mozzicafreddo, Matteo
Cuccioloni, Massimiliano
Angeletti, Mauro
Ayub, Nicolás Daniel
author_role author
author2 Stritzler, Margarita
Lisi, Christian Daniel
Alleva, Karina Edith
Pagano, María Elba
Ardila, Fernando
Mozzicafreddo, Matteo
Cuccioloni, Massimiliano
Angeletti, Mauro
Ayub, Nicolás Daniel
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ABIOTIC STRESS
ACETOACETYL-COA THIOLASE
ISOPRENOID
MVA PATHWAY
THIOLASE II
topic ABIOTIC STRESS
ACETOACETYL-COA THIOLASE
ISOPRENOID
MVA PATHWAY
THIOLASE II
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Acetoacetyl-CoA thiolase (EC 2.3.1.9), also called thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA. This is the first enzymatic step in the biosynthesis of isoprenoids via mevalonate (MVA). In this work, thiolase II from alfalfa (MsAACT1) was identified and cloned. The enzymatic activity was experimentally demonstrated in planta and in heterologous systems. The condensation reaction by MsAACT1 was proved to be inhibited by CoA suggesting a negative feedback regulation of isoprenoid production. Real-time RT-PCR analysis indicated that MsAACT1 expression is highly increased in roots and leaves under cold and salinity stress. Treatment with mevastatin, a specific inhibitor of the MVA pathway, resulted in a decrease in squalene production, antioxidant activity, and the survival of stressed plants. As expected, the presence of mevastatin did not change chlorophyll and carotenoid levels, isoprenoids synthesized via the plastidial MVA-independent pathway. The addition of vitamin C suppressed the sensitive phenotype of plants challenged with mevastatin, suggesting a critical function of the MVA pathway in abiotic stress-inducible antioxidant defence. MsAACT1 over-expressing transgenic plants showed salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without altering the 3-hydroxy-3-methylglutaryl- CoA reductase (HMGR) activity in salt-stress conditions. Thus, acetoacetyl-CoA thiolase is a regulatory enzyme in isoprenoid biosynthesis involved in abiotic stress adaptation.
Fil: Soto, Gabriela Cynthia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Stritzler, Margarita. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lisi, Christian Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Alleva, Karina Edith. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Biodiversidad y Biología Experimental; Argentina
Fil: Pagano, María Elba. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
Fil: Ardila, Fernando. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Mozzicafreddo, Matteo. Universita Degli Di Camerino; Italia
Fil: Cuccioloni, Massimiliano. Universita Degli Di Camerino; Italia
Fil: Angeletti, Mauro. Universita Degli Di Camerino; Italia
Fil: Ayub, Nicolás Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas; Argentina
description Acetoacetyl-CoA thiolase (EC 2.3.1.9), also called thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA. This is the first enzymatic step in the biosynthesis of isoprenoids via mevalonate (MVA). In this work, thiolase II from alfalfa (MsAACT1) was identified and cloned. The enzymatic activity was experimentally demonstrated in planta and in heterologous systems. The condensation reaction by MsAACT1 was proved to be inhibited by CoA suggesting a negative feedback regulation of isoprenoid production. Real-time RT-PCR analysis indicated that MsAACT1 expression is highly increased in roots and leaves under cold and salinity stress. Treatment with mevastatin, a specific inhibitor of the MVA pathway, resulted in a decrease in squalene production, antioxidant activity, and the survival of stressed plants. As expected, the presence of mevastatin did not change chlorophyll and carotenoid levels, isoprenoids synthesized via the plastidial MVA-independent pathway. The addition of vitamin C suppressed the sensitive phenotype of plants challenged with mevastatin, suggesting a critical function of the MVA pathway in abiotic stress-inducible antioxidant defence. MsAACT1 over-expressing transgenic plants showed salinity tolerance comparable with empty vector transformed plants and enhanced production of squalene without altering the 3-hydroxy-3-methylglutaryl- CoA reductase (HMGR) activity in salt-stress conditions. Thus, acetoacetyl-CoA thiolase is a regulatory enzyme in isoprenoid biosynthesis involved in abiotic stress adaptation.
publishDate 2011
dc.date.none.fl_str_mv 2011-11
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/11336/114222
Soto, Gabriela Cynthia; Stritzler, Margarita; Lisi, Christian Daniel; Alleva, Karina Edith; Pagano, María Elba; et al.; Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation; Oxford University Press; Journal of Experimental Botany; 62; 15; 11-2011; 5699-5711
0022-0957
CONICET Digital
CONICET
url http://hdl.handle.net/11336/114222
identifier_str_mv Soto, Gabriela Cynthia; Stritzler, Margarita; Lisi, Christian Daniel; Alleva, Karina Edith; Pagano, María Elba; et al.; Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptation; Oxford University Press; Journal of Experimental Botany; 62; 15; 11-2011; 5699-5711
0022-0957
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://academic.oup.com/jxb/article/62/15/5699/563304
info:eu-repo/semantics/altIdentifier/doi/10.1093/jxb/err287
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 Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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 12.993085

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