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

Autores
Soto, G.; Stritzler, M.; Lisi, C.; Alleva, K.; Pagano, M.E.; Ardila, F.; Mozzicafreddo, M.; Cuccioloni, M.; Angeletti, M.; Ayub, N.D.
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. © 2011 The Author.
Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Stritzler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Ardila, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
J. Exp. Bot. 2011;62(15):5699-5711
Materia
Abiotic stress
acetoacetyl-CoA thiolase
isoprenoid
MVA pathway
thiolase II
acetyl coenzyme A acetyltransferase
mevalonic acid
pravastatin
squalene
vegetable protein
alfalfa
article
drug effect
genetics
metabolism
plant leaf
plant root
real time polymerase chain reaction
signal transduction
transgenic plant
Acetyl-CoA C-Acetyltransferase
Medicago sativa
Mevalonic Acid
Plant Leaves
Plant Proteins
Plant Roots
Plants, Genetically Modified
Pravastatin
Real-Time Polymerase Chain Reaction
Signal Transduction
Squalene
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00220957_v62_n15_p5699_Soto

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oai_identifier_str paperaa:paper_00220957_v62_n15_p5699_Soto
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Acetoacetyl-CoA thiolase regulates the mevalonate pathway during abiotic stress adaptationSoto, G.Stritzler, M.Lisi, C.Alleva, K.Pagano, M.E.Ardila, F.Mozzicafreddo, M.Cuccioloni, M.Angeletti, M.Ayub, N.D.Abiotic stressacetoacetyl-CoA thiolaseisoprenoidMVA pathwaythiolase IIacetyl coenzyme A acetyltransferasemevalonic acidpravastatinsqualenevegetable proteinalfalfaarticledrug effectgeneticsmetabolismplant leafplant rootreal time polymerase chain reactionsignal transductiontransgenic plantAcetyl-CoA C-AcetyltransferaseMedicago sativaMevalonic AcidPlant LeavesPlant ProteinsPlant RootsPlants, Genetically ModifiedPravastatinReal-Time Polymerase Chain ReactionSignal TransductionSqualeneAcetoacetyl-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. © 2011 The Author.Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Stritzler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Ardila, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00220957_v62_n15_p5699_SotoJ. Exp. Bot. 2011;62(15):5699-5711reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-18T10:09:26Zpaperaa:paper_00220957_v62_n15_p5699_SotoInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-18 10:09:27.389Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
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, G.
Abiotic stress
acetoacetyl-CoA thiolase
isoprenoid
MVA pathway
thiolase II
acetyl coenzyme A acetyltransferase
mevalonic acid
pravastatin
squalene
vegetable protein
alfalfa
article
drug effect
genetics
metabolism
plant leaf
plant root
real time polymerase chain reaction
signal transduction
transgenic plant
Acetyl-CoA C-Acetyltransferase
Medicago sativa
Mevalonic Acid
Plant Leaves
Plant Proteins
Plant Roots
Plants, Genetically Modified
Pravastatin
Real-Time Polymerase Chain Reaction
Signal Transduction
Squalene
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, G.
Stritzler, M.
Lisi, C.
Alleva, K.
Pagano, M.E.
Ardila, F.
Mozzicafreddo, M.
Cuccioloni, M.
Angeletti, M.
Ayub, N.D.
author Soto, G.
author_facet Soto, G.
Stritzler, M.
Lisi, C.
Alleva, K.
Pagano, M.E.
Ardila, F.
Mozzicafreddo, M.
Cuccioloni, M.
Angeletti, M.
Ayub, N.D.
author_role author
author2 Stritzler, M.
Lisi, C.
Alleva, K.
Pagano, M.E.
Ardila, F.
Mozzicafreddo, M.
Cuccioloni, M.
Angeletti, M.
Ayub, N.D.
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
acetyl coenzyme A acetyltransferase
mevalonic acid
pravastatin
squalene
vegetable protein
alfalfa
article
drug effect
genetics
metabolism
plant leaf
plant root
real time polymerase chain reaction
signal transduction
transgenic plant
Acetyl-CoA C-Acetyltransferase
Medicago sativa
Mevalonic Acid
Plant Leaves
Plant Proteins
Plant Roots
Plants, Genetically Modified
Pravastatin
Real-Time Polymerase Chain Reaction
Signal Transduction
Squalene
topic Abiotic stress
acetoacetyl-CoA thiolase
isoprenoid
MVA pathway
thiolase II
acetyl coenzyme A acetyltransferase
mevalonic acid
pravastatin
squalene
vegetable protein
alfalfa
article
drug effect
genetics
metabolism
plant leaf
plant root
real time polymerase chain reaction
signal transduction
transgenic plant
Acetyl-CoA C-Acetyltransferase
Medicago sativa
Mevalonic Acid
Plant Leaves
Plant Proteins
Plant Roots
Plants, Genetically Modified
Pravastatin
Real-Time Polymerase Chain Reaction
Signal Transduction
Squalene
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. © 2011 The Author.
Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Stritzler, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Ardila, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Ayub, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; 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. © 2011 The Author.
publishDate 2011
dc.date.none.fl_str_mv 2011
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/20.500.12110/paper_00220957_v62_n15_p5699_Soto
url http://hdl.handle.net/20.500.12110/paper_00220957_v62_n15_p5699_Soto
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv J. Exp. Bot. 2011;62(15):5699-5711
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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