Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex

Enterococcus faecalis encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which is constituted by four subunits: E. faecalis carboxyltransferase subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and the novel subunit Ef-H. Our results show that in E. faecalis, su...

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Detalhes bibliográficos
Autores: Repizo, Guillermo Daniel, Blancato, Victor Sebastian, Mortera, Pablo, Lolkema, Juke, Magni, Christian
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:Argentina
Recursos:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/104575
Acesso em linha:http://hdl.handle.net/11336/104575
Access Level:acceso abierto
Palavra-chave:ENTEROCOCCUS
OXALOACETATE
DECARBOXILASE
CITRATE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
id AR_548fdcee5bf0c83b50aa119c8335eb67
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network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
title Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
spellingShingle Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
Repizo, Guillermo Daniel
ENTEROCOCCUS
OXALOACETATE
DECARBOXILASE
CITRATE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
title_full Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
title_fullStr Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
title_full_unstemmed Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
title_sort Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex
dc.creator.none.fl_str_mv Repizo, Guillermo Daniel
Blancato, Victor Sebastian
Mortera, Pablo
Lolkema, Juke
Magni, Christian
author Repizo, Guillermo Daniel
author_facet Repizo, Guillermo Daniel
Blancato, Victor Sebastian
Mortera, Pablo
Lolkema, Juke
Magni, Christian
author_role author
author2 Blancato, Victor Sebastian
Mortera, Pablo
Lolkema, Juke
Magni, Christian
author2_role author
author
author
author
dc.subject.none.fl_str_mv ENTEROCOCCUS
OXALOACETATE
DECARBOXILASE
CITRATE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic ENTEROCOCCUS
OXALOACETATE
DECARBOXILASE
CITRATE
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
description Enterococcus faecalis encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which is constituted by four subunits: E. faecalis carboxyltransferase subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and the novel subunit Ef-H. Our results show that in E. faecalis, subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex (termed Ef-AHD) which is also associated with the membrane. In order to characterize the role of the novel Ef-H subunit, coexpression of oad genes was performed in Escherichia coli, showing that this subunit is vital for Ef-A and Ef-D interaction. Diminished growth of the oadA and oadD single deletion mutants in citrate-supplemented medium indicated that the activity of the complex is essential for citrate utilization. Remarkably, the oadB-deficient strain was still capable of growing to wild-type levels but with a delay during the citrate-consuming phase, suggesting that the soluble Ef-AHD complex is functional in E. faecalis. These results suggest that the Ef-AHD complex is active in its soluble form, and that it is capable of interacting in a dynamic way with the membrane-bound Ef-B subunit to achieve its maximal alkalinization capacity during citrate fermentation.
publishDate 2013
dc.date.none.fl_str_mv 2013-05
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/11336/104575
Repizo, Guillermo Daniel; Blancato, Victor Sebastian; Mortera, Pablo; Lolkema, Juke; Magni, Christian; Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex; American Society for Microbiology; Applied And Environmental Microbiology; 79; 9; 5-2013; 2882-2890
0099-2240
CONICET Digital
CONICET
url http://hdl.handle.net/11336/104575
identifier_str_mv Repizo, Guillermo Daniel; Blancato, Victor Sebastian; Mortera, Pablo; Lolkema, Juke; Magni, Christian; Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex; American Society for Microbiology; Applied And Environmental Microbiology; 79; 9; 5-2013; 2882-2890
0099-2240
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://aem.asm.org/content/79/9/2882.long
info:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.03980-12
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623145/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/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 American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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
_version_ 1799195678032789504
spelling Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complexRepizo, Guillermo DanielBlancato, Victor SebastianMortera, PabloLolkema, JukeMagni, ChristianENTEROCOCCUSOXALOACETATEDECARBOXILASECITRATEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Enterococcus faecalis encodes a biotin-dependent oxaloacetate decarboxylase (OAD), which is constituted by four subunits: E. faecalis carboxyltransferase subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and the novel subunit Ef-H. Our results show that in E. faecalis, subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex (termed Ef-AHD) which is also associated with the membrane. In order to characterize the role of the novel Ef-H subunit, coexpression of oad genes was performed in Escherichia coli, showing that this subunit is vital for Ef-A and Ef-D interaction. Diminished growth of the oadA and oadD single deletion mutants in citrate-supplemented medium indicated that the activity of the complex is essential for citrate utilization. Remarkably, the oadB-deficient strain was still capable of growing to wild-type levels but with a delay during the citrate-consuming phase, suggesting that the soluble Ef-AHD complex is functional in E. faecalis. These results suggest that the Ef-AHD complex is active in its soluble form, and that it is capable of interacting in a dynamic way with the membrane-bound Ef-B subunit to achieve its maximal alkalinization capacity during citrate fermentation.Fil: Repizo, Guillermo Daniel. 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. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; ArgentinaFil: Blancato, Victor Sebastian. 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. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; ArgentinaFil: Mortera, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina. 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. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; ArgentinaFil: Lolkema, Juke. University of Groningen; Países BajosFil: Magni, Christian. 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. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología; ArgentinaAmerican Society for Microbiology2013-05info: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/11336/104575Repizo, Guillermo Daniel; Blancato, Victor Sebastian; Mortera, Pablo; Lolkema, Juke; Magni, Christian; Biochemical and genetic characterization of the Enterococcus faecalis Oxaloacetate decarboxylase complex; American Society for Microbiology; Applied And Environmental Microbiology; 79; 9; 5-2013; 2882-28900099-2240CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://aem.asm.org/content/79/9/2882.longinfo:eu-repo/semantics/altIdentifier/doi/10.1128/AEM.03980-12info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623145/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:59:59Zoai:ri.conicet.gov.ar:11336/104575instacron: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:34982024-05-08 14:00:00.096CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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