Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases

Autores
Scattolini, Albertina; Costa, Joaquin; Pianessi, Tulio L.; Uttaro, Antonio Domingo; Mansilla, Maria Cecilia
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipoylation is a post-translational modification in which lipoic acid is attached to specific apoproteins of enzyme complexes, like E2 subunits of dehydrogenases or GcvH of the glycine cleavage system. A defining feature of organisms with a lipoyl-relay system is the presence of amidotransferase activity, which enables the transfer of lipoyl groups attached to intermediary proteins to the E2 subunits. In this study, we characterized the lipoate metabolism of Capsaspora owczarzaki and Plasmodium falciparum. Both organisms utilize amidotransferases in their lipoylation pathways, with the filasterian enzyme playing a key role in lipoate synthesis, while the apicomplexan counterpart, previously considered a lipoyltransferase, is essential in its lipoate salvage pathway. We also discovered that specific structural features and certain conserved domains in eukaryotic amidotransferases can significantly influence their mechanism of action and susceptibility to the lipoate analog bromooctanoate. Overall, this study highlights the metabolic strategies of C. owczarzaki and emphasizes the critical role of amidotransferases as ancestral enzymes in the evolution of lipoate metabolism, suggesting that the lipoyl relay may represent a universal pathway across diverse clades.
Fil: Scattolini, Albertina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Costa, Joaquin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Pianessi, Tulio L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Uttaro, Antonio Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Mansilla, Maria Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
AMIDOTRANSFERASE
ANTIMICROBIAL
CAPSASPORA
LIPOIC ACID
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:11336/265036
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/265036
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferasesScattolini, AlbertinaCosta, JoaquinPianessi, Tulio L.Uttaro, Antonio DomingoMansilla, Maria CeciliaAMIDOTRANSFERASEANTIMICROBIALCAPSASPORALIPOIC ACIDhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Lipoylation is a post-translational modification in which lipoic acid is attached to specific apoproteins of enzyme complexes, like E2 subunits of dehydrogenases or GcvH of the glycine cleavage system. A defining feature of organisms with a lipoyl-relay system is the presence of amidotransferase activity, which enables the transfer of lipoyl groups attached to intermediary proteins to the E2 subunits. In this study, we characterized the lipoate metabolism of Capsaspora owczarzaki and Plasmodium falciparum. Both organisms utilize amidotransferases in their lipoylation pathways, with the filasterian enzyme playing a key role in lipoate synthesis, while the apicomplexan counterpart, previously considered a lipoyltransferase, is essential in its lipoate salvage pathway. We also discovered that specific structural features and certain conserved domains in eukaryotic amidotransferases can significantly influence their mechanism of action and susceptibility to the lipoate analog bromooctanoate. Overall, this study highlights the metabolic strategies of C. owczarzaki and emphasizes the critical role of amidotransferases as ancestral enzymes in the evolution of lipoate metabolism, suggesting that the lipoyl relay may represent a universal pathway across diverse clades.Fil: Scattolini, Albertina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Costa, Joaquin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Pianessi, Tulio L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Uttaro, Antonio Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Mansilla, Maria Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaWiley Blackwell Publishing, Inc2024-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/265036Scattolini, Albertina; Costa, Joaquin; Pianessi, Tulio L.; Uttaro, Antonio Domingo; Mansilla, Maria Cecilia; Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 2024; 12-2024; 1-230950-382XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.authorea.com/users/872691/articles/1253178-impairment-of-lipoylation-mediated-by-bromooctanoate-targets-eukaryotic-amidotransferasesinfo:eu-repo/semantics/altIdentifier/doi/10.22541/au.173463331.18754625/v1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:25Zoai:ri.conicet.gov.ar:11336/265036instacron: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:34982025-09-03 10:06:25.818CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
title Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
spellingShingle Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
Scattolini, Albertina
AMIDOTRANSFERASE
ANTIMICROBIAL
CAPSASPORA
LIPOIC ACID
title_short Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
title_full Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
title_fullStr Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
title_full_unstemmed Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
title_sort Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases
dc.creator.none.fl_str_mv Scattolini, Albertina
Costa, Joaquin
Pianessi, Tulio L.
Uttaro, Antonio Domingo
Mansilla, Maria Cecilia
author Scattolini, Albertina
author_facet Scattolini, Albertina
Costa, Joaquin
Pianessi, Tulio L.
Uttaro, Antonio Domingo
Mansilla, Maria Cecilia
author_role author
author2 Costa, Joaquin
Pianessi, Tulio L.
Uttaro, Antonio Domingo
Mansilla, Maria Cecilia
author2_role author
author
author
author
dc.subject.none.fl_str_mv AMIDOTRANSFERASE
ANTIMICROBIAL
CAPSASPORA
LIPOIC ACID
topic AMIDOTRANSFERASE
ANTIMICROBIAL
CAPSASPORA
LIPOIC ACID
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Lipoylation is a post-translational modification in which lipoic acid is attached to specific apoproteins of enzyme complexes, like E2 subunits of dehydrogenases or GcvH of the glycine cleavage system. A defining feature of organisms with a lipoyl-relay system is the presence of amidotransferase activity, which enables the transfer of lipoyl groups attached to intermediary proteins to the E2 subunits. In this study, we characterized the lipoate metabolism of Capsaspora owczarzaki and Plasmodium falciparum. Both organisms utilize amidotransferases in their lipoylation pathways, with the filasterian enzyme playing a key role in lipoate synthesis, while the apicomplexan counterpart, previously considered a lipoyltransferase, is essential in its lipoate salvage pathway. We also discovered that specific structural features and certain conserved domains in eukaryotic amidotransferases can significantly influence their mechanism of action and susceptibility to the lipoate analog bromooctanoate. Overall, this study highlights the metabolic strategies of C. owczarzaki and emphasizes the critical role of amidotransferases as ancestral enzymes in the evolution of lipoate metabolism, suggesting that the lipoyl relay may represent a universal pathway across diverse clades.
Fil: Scattolini, Albertina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Costa, Joaquin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Pianessi, Tulio L.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Uttaro, Antonio Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Mansilla, Maria Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description Lipoylation is a post-translational modification in which lipoic acid is attached to specific apoproteins of enzyme complexes, like E2 subunits of dehydrogenases or GcvH of the glycine cleavage system. A defining feature of organisms with a lipoyl-relay system is the presence of amidotransferase activity, which enables the transfer of lipoyl groups attached to intermediary proteins to the E2 subunits. In this study, we characterized the lipoate metabolism of Capsaspora owczarzaki and Plasmodium falciparum. Both organisms utilize amidotransferases in their lipoylation pathways, with the filasterian enzyme playing a key role in lipoate synthesis, while the apicomplexan counterpart, previously considered a lipoyltransferase, is essential in its lipoate salvage pathway. We also discovered that specific structural features and certain conserved domains in eukaryotic amidotransferases can significantly influence their mechanism of action and susceptibility to the lipoate analog bromooctanoate. Overall, this study highlights the metabolic strategies of C. owczarzaki and emphasizes the critical role of amidotransferases as ancestral enzymes in the evolution of lipoate metabolism, suggesting that the lipoyl relay may represent a universal pathway across diverse clades.
publishDate 2024
dc.date.none.fl_str_mv 2024-12
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/11336/265036
Scattolini, Albertina; Costa, Joaquin; Pianessi, Tulio L.; Uttaro, Antonio Domingo; Mansilla, Maria Cecilia; Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 2024; 12-2024; 1-23
0950-382X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/265036
identifier_str_mv Scattolini, Albertina; Costa, Joaquin; Pianessi, Tulio L.; Uttaro, Antonio Domingo; Mansilla, Maria Cecilia; Impairment of lipoylation mediated by bromooctanoate targets eukaryotic amidotransferases; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 2024; 12-2024; 1-23
0950-382X
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://www.authorea.com/users/872691/articles/1253178-impairment-of-lipoylation-mediated-by-bromooctanoate-targets-eukaryotic-amidotransferases
info:eu-repo/semantics/altIdentifier/doi/10.22541/au.173463331.18754625/v1
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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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