Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches

Autores
Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; Angeletti, Mauro; Salerno, Juan Carlos; Ayub, Nicolas Daniel
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.
Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Thiolase Ii
Coa
Acetyl-Coa
Tricarboxyl Acid Cycle
Antioxidant Compounds
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/4037

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approachesFox, Ana RominaSoto, Gabriela CynthiaMozzicafreddo, MatteoGarcía, Araceli NoraCuccioloni, MassimilianoAngeletti, MauroSalerno, Juan CarlosAyub, Nicolas DanielThiolase IiCoaAcetyl-CoaTricarboxyl Acid CycleAntioxidant Compoundshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; ArgentinaFil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; ArgentinaFil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; ArgentinaFil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; ItaliaFil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; ArgentinaFil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2013-10-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4037Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-100378-1119enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378111913013164info:eu-repo/semantics/altIdentifier/doi/10.1016/j.gene.2013.09.096info:eu-repo/semantics/altIdentifier/issn/0378-1119info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:35:48Zoai:ri.conicet.gov.ar:11336/4037instacron: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:34982025-10-15 15:35:48.436CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
title Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
spellingShingle Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
Fox, Ana Romina
Thiolase Ii
Coa
Acetyl-Coa
Tricarboxyl Acid Cycle
Antioxidant Compounds
title_short Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
title_full Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
title_fullStr Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
title_full_unstemmed Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
title_sort Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches
dc.creator.none.fl_str_mv Fox, Ana Romina
Soto, Gabriela Cynthia
Mozzicafreddo, Matteo
García, Araceli Nora
Cuccioloni, Massimiliano
Angeletti, Mauro
Salerno, Juan Carlos
Ayub, Nicolas Daniel
author Fox, Ana Romina
author_facet Fox, Ana Romina
Soto, Gabriela Cynthia
Mozzicafreddo, Matteo
García, Araceli Nora
Cuccioloni, Massimiliano
Angeletti, Mauro
Salerno, Juan Carlos
Ayub, Nicolas Daniel
author_role author
author2 Soto, Gabriela Cynthia
Mozzicafreddo, Matteo
García, Araceli Nora
Cuccioloni, Massimiliano
Angeletti, Mauro
Salerno, Juan Carlos
Ayub, Nicolas Daniel
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Thiolase Ii
Coa
Acetyl-Coa
Tricarboxyl Acid Cycle
Antioxidant Compounds
topic Thiolase Ii
Coa
Acetyl-Coa
Tricarboxyl Acid Cycle
Antioxidant Compounds
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), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.
Fil: Fox, Ana Romina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Soto, Gabriela Cynthia. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular; Argentina
Fil: Mozzicafreddo, Matteo. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: García, Araceli Nora. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Cuccioloni, Massimiliano. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Angeletti, Mauro. University of Camerino. School of Biosciences and Biotechnology; Italia
Fil: Salerno, Juan Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina
Fil: Ayub, Nicolas Daniel. Instituto Nacional de Tecnología Agropecuaria. Centro Nacional de Investigaciones Agropecuarias. Centro de Investigación de Ciencias Veterinarias y Agronómicas. Instituto de Genética; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Acetoacetyl-CoA thiolase (EC 2.3.1.9), commonly named thiolase II, condenses two molecules of acetyl-CoA to give acetoacetyl-CoA and CoA. This enzyme acts in anabolic processes as the first step in the biosynthesis of isoprenoids and polyhydroxybutyrate in eukaryotes and bacteria, respectively. We have recently reported the evolutionary and functional equivalence of these enzymes, suggesting that thiolase II could be the rate limiting enzyme in these pathways and presented evidence indicating that this enzyme modulates the availability of reducing equivalents during abiotic stress adaptation in bacteria and plants. However, these results are not sufficient to clarify why thiolase II was evolutionary selected as a critical enzyme in the production of antioxidant compounds. Regarding this intriguing topic, we propose that thiolase II could sense changes in the acetyl-CoA/CoA ratio induced by the inhibition of the tricarboxylic acid cycle under abiotic stress. Thus, the high level of evolutionary and functional constraint of thiolase II may be due to the connection of this enzyme with an ancient and conserved metabolic route.
publishDate 2013
dc.date.none.fl_str_mv 2013-10-11
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/11336/4037
Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-10
0378-1119
url http://hdl.handle.net/11336/4037
identifier_str_mv Fox, Ana Romina; Soto, Gabriela Cynthia; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; et al.; Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches; Elsevier; Gene; 533; 1; 11-10-2013; 5-10
0378-1119
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0378111913013164
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.gene.2013.09.096
info:eu-repo/semantics/altIdentifier/issn/0378-1119
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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