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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_00220957_v62_n15_p5699_Soto
Ver los metadatos del registro completo
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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 |
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instname_str |
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
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UBA-FCEN |
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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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