A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis

Autores
Martin, Natalia; Christensen, Quin H.; Mansilla, Maria Cecilia; Cronan, John E.; de Mendoza, Diego
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Bacillus subtilis genome encodes three apparentlipoyl ligase homologues: yhfJ, yqhM and ywfL,which we have renamed lplJ, lipM and lipLrespectively. We show that LplJ encodes the solelipoyl ligase of this bacterium. Physiological and biochemicalcharacterization of a DlipM strain showedthat LipM is absolutely required for the endogenouslipoylation of all lipoate-dependent proteins, confirmingits role as the B. subtilis octanoyltransferase.However, we also report that in contrast to Escherichiacoli, B. subtilis requires a third protein forlipoic acid assembly, LipL. B. subtilis DlipL strains areunable to synthesize lipoic acid despite the presenceof LipM and the sulphur insertion enzyme, LipA,which should suffice for lipoic acid biosynthesisbased on the E. coli model. LipM is only required forthe endogenous lipoylation pathway, whereas LipLalso plays a role in lipoic acid scavenging. Expressionof E. coli lipB allows growth of B. subtilis DlipL orDlipM strains in the absence of supplements. In contrast,growth of an E. coli DlipB strain can be complementedwith lipM, but not lipL. These data togetherwith those of the companion article provide evidencethat LipM and LipL catalyse sequential reactions in anovel pathway for lipoic acid biosynthesis.
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: Christensen, Quin H.. No especifíca;
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: Cronan, John E.. University of Illinois; Estados Unidos
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
Materia
LIPOIC ACID
BACILLUS SUBTILIS
BIOSYNTHESIS
OCTANOYLTRANSFER
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:11336/268126
Acceder
id CONICETDig_ba915613cce0c7e165a2f879e5eda343
oai_identifier_str oai:ri.conicet.gov.ar:11336/268126
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesisMartin, NataliaChristensen, Quin H.Mansilla, Maria CeciliaCronan, John E.de Mendoza, DiegoLIPOIC ACIDBACILLUS SUBTILISBIOSYNTHESISOCTANOYLTRANSFERhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The Bacillus subtilis genome encodes three apparentlipoyl ligase homologues: yhfJ, yqhM and ywfL,which we have renamed lplJ, lipM and lipLrespectively. We show that LplJ encodes the solelipoyl ligase of this bacterium. Physiological and biochemicalcharacterization of a DlipM strain showedthat LipM is absolutely required for the endogenouslipoylation of all lipoate-dependent proteins, confirmingits role as the B. subtilis octanoyltransferase.However, we also report that in contrast to Escherichiacoli, B. subtilis requires a third protein forlipoic acid assembly, LipL. B. subtilis DlipL strains areunable to synthesize lipoic acid despite the presenceof LipM and the sulphur insertion enzyme, LipA,which should suffice for lipoic acid biosynthesisbased on the E. coli model. LipM is only required forthe endogenous lipoylation pathway, whereas LipLalso plays a role in lipoic acid scavenging. Expressionof E. coli lipB allows growth of B. subtilis DlipL orDlipM strains in the absence of supplements. In contrast,growth of an E. coli DlipB strain can be complementedwith lipM, but not lipL. These data togetherwith those of the companion article provide evidencethat LipM and LipL catalyse sequential reactions in anovel pathway for lipoic acid biosynthesis.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; ArgentinaFil: Christensen, Quin H.. No especifíca;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; ArgentinaFil: Cronan, John E.. University of Illinois; Estados UnidosFil: 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; ArgentinaWiley 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/11336/268126Martin, Natalia; Christensen, Quin H.; Mansilla, Maria Cecilia; Cronan, John E.; de Mendoza, Diego; A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 335-3490950-382XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2011.07597.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2958.2011.07597.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 Técnicas2025-09-03T10:11:12Zoai:ri.conicet.gov.ar:11336/268126instacron: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 10:11:12.303CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
title A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
spellingShingle A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
Martin, Natalia
LIPOIC ACID
BACILLUS SUBTILIS
BIOSYNTHESIS
OCTANOYLTRANSFER
title_short A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
title_full A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
title_fullStr A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
title_full_unstemmed A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
title_sort A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis
dc.creator.none.fl_str_mv Martin, Natalia
Christensen, Quin H.
Mansilla, Maria Cecilia
Cronan, John E.
de Mendoza, Diego
author Martin, Natalia
author_facet Martin, Natalia
Christensen, Quin H.
Mansilla, Maria Cecilia
Cronan, John E.
de Mendoza, Diego
author_role author
author2 Christensen, Quin H.
Mansilla, Maria Cecilia
Cronan, John E.
de Mendoza, Diego
author2_role author
author
author
author
dc.subject.none.fl_str_mv LIPOIC ACID
BACILLUS SUBTILIS
BIOSYNTHESIS
OCTANOYLTRANSFER
topic LIPOIC ACID
BACILLUS SUBTILIS
BIOSYNTHESIS
OCTANOYLTRANSFER
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The Bacillus subtilis genome encodes three apparentlipoyl ligase homologues: yhfJ, yqhM and ywfL,which we have renamed lplJ, lipM and lipLrespectively. We show that LplJ encodes the solelipoyl ligase of this bacterium. Physiological and biochemicalcharacterization of a DlipM strain showedthat LipM is absolutely required for the endogenouslipoylation of all lipoate-dependent proteins, confirmingits role as the B. subtilis octanoyltransferase.However, we also report that in contrast to Escherichiacoli, B. subtilis requires a third protein forlipoic acid assembly, LipL. B. subtilis DlipL strains areunable to synthesize lipoic acid despite the presenceof LipM and the sulphur insertion enzyme, LipA,which should suffice for lipoic acid biosynthesisbased on the E. coli model. LipM is only required forthe endogenous lipoylation pathway, whereas LipLalso plays a role in lipoic acid scavenging. Expressionof E. coli lipB allows growth of B. subtilis DlipL orDlipM strains in the absence of supplements. In contrast,growth of an E. coli DlipB strain can be complementedwith lipM, but not lipL. These data togetherwith those of the companion article provide evidencethat LipM and LipL catalyse sequential reactions in anovel pathway for lipoic acid biosynthesis.
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: Christensen, Quin H.. No especifíca;
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: Cronan, John E.. University of Illinois; Estados Unidos
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
description The Bacillus subtilis genome encodes three apparentlipoyl ligase homologues: yhfJ, yqhM and ywfL,which we have renamed lplJ, lipM and lipLrespectively. We show that LplJ encodes the solelipoyl ligase of this bacterium. Physiological and biochemicalcharacterization of a DlipM strain showedthat LipM is absolutely required for the endogenouslipoylation of all lipoate-dependent proteins, confirmingits role as the B. subtilis octanoyltransferase.However, we also report that in contrast to Escherichiacoli, B. subtilis requires a third protein forlipoic acid assembly, LipL. B. subtilis DlipL strains areunable to synthesize lipoic acid despite the presenceof LipM and the sulphur insertion enzyme, LipA,which should suffice for lipoic acid biosynthesisbased on the E. coli model. LipM is only required forthe endogenous lipoylation pathway, whereas LipLalso plays a role in lipoic acid scavenging. Expressionof E. coli lipB allows growth of B. subtilis DlipL orDlipM strains in the absence of supplements. In contrast,growth of an E. coli DlipB strain can be complementedwith lipM, but not lipL. These data togetherwith those of the companion article provide evidencethat LipM and LipL catalyse sequential reactions in anovel pathway for lipoic acid biosynthesis.
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/11336/268126
Martin, Natalia; Christensen, Quin H.; Mansilla, Maria Cecilia; Cronan, John E.; de Mendoza, Diego; A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 335-349
0950-382X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/268126
identifier_str_mv Martin, Natalia; Christensen, Quin H.; Mansilla, Maria Cecilia; Cronan, John E.; de Mendoza, Diego; A novel two‐gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 80; 2; 3-2011; 335-349
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.1365-2958.2011.07597.x
info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2958.2011.07597.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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