A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis

Autores
Christensen, Quin H.; Martin, Natalia; Mansilla, Maria Cecilia; de Mendoza, Diego; Cronan, John E.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In the companion paper we reported that Bacillussubtilis requires three proteins for lipoic acid metabolism,all of which are members of the lipoate proteinligase family. Two of the proteins, LipM and LplJ, havebeen shown to be an octanoyltransferase and alipoate : protein ligase respectively. The third protein,LipL, is essential for lipoic acid synthesis, but hadno detectable octanoyltransferase or ligase activityeither in vitro or in vivo. We report that LipM specificallymodifies the glycine cleavage system protein,GcvH, and therefore another mechanism mustexist for modification of other lipoic acid requiringenzymes (e.g. pyruvate dehydrogenase). We showthat this function is provided by LipL, which catalysesthe amidotransfer (transamidation) of the octanoylmoiety from octanoyl-GcvH to the E2 subunit of pyruvatedehydrogenase. LipL activity was demonstratedin vitro with purified components and proceeds via athioester-linked acyl-enzyme intermediate. As predicted,DgcvH strains are lipoate auxotrophs. LipLrepresents a new enzyme activity. It is a GcvH:[lipoyldomain] amidotransferase that probably uses a Cys-Lys catalytic dyad. Although the active site cysteineresidues of LipL and LipB are located in differentpositions within the polypeptide chains, alignment oftheir structures show these residues occupy similarpositions. Thus, these two homologous enzymeshave convergent architectures.
Fil: Christensen, Quin H.. University of Illinois; Estados Unidos
Fil: Martin, Natalia. 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
Fil: de Mendoza, Diego. 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: Cronan, John E.. University of Illinois; Estados Unidos
Materia
LIPOIC ACID
BACILLUS SUBTILIS
AMIDOTRANSFERASE
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:11336/268219
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/268219
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilisChristensen, Quin H.Martin, NataliaMansilla, Maria Ceciliade Mendoza, DiegoCronan, John E.LIPOIC ACIDBACILLUS SUBTILISAMIDOTRANSFERASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In the companion paper we reported that Bacillussubtilis requires three proteins for lipoic acid metabolism,all of which are members of the lipoate proteinligase family. Two of the proteins, LipM and LplJ, havebeen shown to be an octanoyltransferase and alipoate : protein ligase respectively. The third protein,LipL, is essential for lipoic acid synthesis, but hadno detectable octanoyltransferase or ligase activityeither in vitro or in vivo. We report that LipM specificallymodifies the glycine cleavage system protein,GcvH, and therefore another mechanism mustexist for modification of other lipoic acid requiringenzymes (e.g. pyruvate dehydrogenase). We showthat this function is provided by LipL, which catalysesthe amidotransfer (transamidation) of the octanoylmoiety from octanoyl-GcvH to the E2 subunit of pyruvatedehydrogenase. LipL activity was demonstratedin vitro with purified components and proceeds via athioester-linked acyl-enzyme intermediate. As predicted,DgcvH strains are lipoate auxotrophs. LipLrepresents a new enzyme activity. It is a GcvH:[lipoyldomain] amidotransferase that probably uses a Cys-Lys catalytic dyad. Although the active site cysteineresidues of LipL and LipB are located in differentpositions within the polypeptide chains, alignment oftheir structures show these residues occupy similarpositions. Thus, these two homologous enzymeshave convergent architectures.Fil: Christensen, Quin H.. University of Illinois; Estados UnidosFil: Martin, Natalia. 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; ArgentinaFil: de Mendoza, Diego. 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: Cronan, John E.. University of Illinois; Estados UnidosWiley Blackwell Publishing, Inc2011-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/268219Christensen, Quin H.; Martin, Natalia; Mansilla, Maria Cecilia; de Mendoza, Diego; Cronan, John E.; A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 350-3630950-382XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07598.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2958.2011.07598.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:07:48Zoai:ri.conicet.gov.ar:11336/268219instacron: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 10:07:48.643CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
title A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
spellingShingle A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
Christensen, Quin H.
LIPOIC ACID
BACILLUS SUBTILIS
AMIDOTRANSFERASE
title_short A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
title_full A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
title_fullStr A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
title_full_unstemmed A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
title_sort A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis
dc.creator.none.fl_str_mv Christensen, Quin H.
Martin, Natalia
Mansilla, Maria Cecilia
de Mendoza, Diego
Cronan, John E.
author Christensen, Quin H.
author_facet Christensen, Quin H.
Martin, Natalia
Mansilla, Maria Cecilia
de Mendoza, Diego
Cronan, John E.
author_role author
author2 Martin, Natalia
Mansilla, Maria Cecilia
de Mendoza, Diego
Cronan, John E.
author2_role author
author
author
author
dc.subject.none.fl_str_mv LIPOIC ACID
BACILLUS SUBTILIS
AMIDOTRANSFERASE
topic LIPOIC ACID
BACILLUS SUBTILIS
AMIDOTRANSFERASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In the companion paper we reported that Bacillussubtilis requires three proteins for lipoic acid metabolism,all of which are members of the lipoate proteinligase family. Two of the proteins, LipM and LplJ, havebeen shown to be an octanoyltransferase and alipoate : protein ligase respectively. The third protein,LipL, is essential for lipoic acid synthesis, but hadno detectable octanoyltransferase or ligase activityeither in vitro or in vivo. We report that LipM specificallymodifies the glycine cleavage system protein,GcvH, and therefore another mechanism mustexist for modification of other lipoic acid requiringenzymes (e.g. pyruvate dehydrogenase). We showthat this function is provided by LipL, which catalysesthe amidotransfer (transamidation) of the octanoylmoiety from octanoyl-GcvH to the E2 subunit of pyruvatedehydrogenase. LipL activity was demonstratedin vitro with purified components and proceeds via athioester-linked acyl-enzyme intermediate. As predicted,DgcvH strains are lipoate auxotrophs. LipLrepresents a new enzyme activity. It is a GcvH:[lipoyldomain] amidotransferase that probably uses a Cys-Lys catalytic dyad. Although the active site cysteineresidues of LipL and LipB are located in differentpositions within the polypeptide chains, alignment oftheir structures show these residues occupy similarpositions. Thus, these two homologous enzymeshave convergent architectures.
Fil: Christensen, Quin H.. University of Illinois; Estados Unidos
Fil: Martin, Natalia. 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
Fil: de Mendoza, Diego. 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: Cronan, John E.. University of Illinois; Estados Unidos
description In the companion paper we reported that Bacillussubtilis requires three proteins for lipoic acid metabolism,all of which are members of the lipoate proteinligase family. Two of the proteins, LipM and LplJ, havebeen shown to be an octanoyltransferase and alipoate : protein ligase respectively. The third protein,LipL, is essential for lipoic acid synthesis, but hadno detectable octanoyltransferase or ligase activityeither in vitro or in vivo. We report that LipM specificallymodifies the glycine cleavage system protein,GcvH, and therefore another mechanism mustexist for modification of other lipoic acid requiringenzymes (e.g. pyruvate dehydrogenase). We showthat this function is provided by LipL, which catalysesthe amidotransfer (transamidation) of the octanoylmoiety from octanoyl-GcvH to the E2 subunit of pyruvatedehydrogenase. LipL activity was demonstratedin vitro with purified components and proceeds via athioester-linked acyl-enzyme intermediate. As predicted,DgcvH strains are lipoate auxotrophs. LipLrepresents a new enzyme activity. It is a GcvH:[lipoyldomain] amidotransferase that probably uses a Cys-Lys catalytic dyad. Although the active site cysteineresidues of LipL and LipB are located in differentpositions within the polypeptide chains, alignment oftheir structures show these residues occupy similarpositions. Thus, these two homologous enzymeshave convergent architectures.
publishDate 2011
dc.date.none.fl_str_mv 2011-03
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/11336/268219
Christensen, Quin H.; Martin, Natalia; Mansilla, Maria Cecilia; de Mendoza, Diego; Cronan, John E.; A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 350-363
0950-382X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/268219
identifier_str_mv Christensen, Quin H.; Martin, Natalia; Mansilla, Maria Cecilia; de Mendoza, Diego; Cronan, John E.; A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 350-363
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://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07598.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2958.2011.07598.x
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
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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score 13.13397

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