A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity

Autores
Ferreyra, Raul Gabriel; Burgardt, Noelia Ines; Milikowski, Daniel; Melen, Gustavo; Kornblihtt, Alberto Rodolfo; Dell Angelica, Esteban; Santomé, José A.; Ermacora, Mario Roberto
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The 14-kDa sterol carrier protein 2 (SCP2) domain is present in Eukaria, Bacteria and Archaea, and has been implicated in the transport and metabolism of lipids. We report the cloning, expression, purification and physicochemical characterization of a SCP2 from the yeast Yarrowia lipolytica (YLSCP2). Analytical size-exclusion chromatography, circular dichroism and fluorescence spectra, indicate that recombinant YLSCP2 is a well-folded monomer. Thermal unfolding experiments show that SCP2 maximal stability is at pH 7.0–9.0. YLSCP2 binds cis-parinaric acid and palmitoyl-CoA with KD values of 81 ± 40 nM and 73 ± 33 nM, respectively, sustaining for the first time the binding of fatty acids and their CoA esters to a nonanimal SCP2. The role of yeast SCP2 and other lipid binding proteins in transport, storage and peroxisomal oxidation of fatty acids is discussed.
Fil: Ferreyra, Raul Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Burgardt, Noelia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Milikowski, Daniel. Universidad Nacional de Quilmes; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Melen, Gustavo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Kornblihtt, Alberto Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Dell Angelica, Esteban. University of California at Los Angeles; Estados Unidos
Fil: Santomé, José A.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Materia
Yeast
Sterol carrier protein
Yarrowia lipolytica
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:11336/248325

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network_name_str CONICET Digital (CONICET)
spelling A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activityFerreyra, Raul GabrielBurgardt, Noelia InesMilikowski, DanielMelen, GustavoKornblihtt, Alberto RodolfoDell Angelica, EstebanSantomé, José A.Ermacora, Mario RobertoYeastSterol carrier proteinYarrowia lipolyticahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 14-kDa sterol carrier protein 2 (SCP2) domain is present in Eukaria, Bacteria and Archaea, and has been implicated in the transport and metabolism of lipids. We report the cloning, expression, purification and physicochemical characterization of a SCP2 from the yeast Yarrowia lipolytica (YLSCP2). Analytical size-exclusion chromatography, circular dichroism and fluorescence spectra, indicate that recombinant YLSCP2 is a well-folded monomer. Thermal unfolding experiments show that SCP2 maximal stability is at pH 7.0–9.0. YLSCP2 binds cis-parinaric acid and palmitoyl-CoA with KD values of 81 ± 40 nM and 73 ± 33 nM, respectively, sustaining for the first time the binding of fatty acids and their CoA esters to a nonanimal SCP2. The role of yeast SCP2 and other lipid binding proteins in transport, storage and peroxisomal oxidation of fatty acids is discussed.Fil: Ferreyra, Raul Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Burgardt, Noelia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Milikowski, Daniel. Universidad Nacional de Quilmes; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Melen, Gustavo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Kornblihtt, Alberto Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Dell Angelica, Esteban. University of California at Los Angeles; Estados UnidosFil: Santomé, José A.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; ArgentinaFil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; ArgentinaElsevier Science Inc.2006-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/248325Ferreyra, Raul Gabriel; Burgardt, Noelia Ines; Milikowski, Daniel; Melen, Gustavo; Kornblihtt, Alberto Rodolfo; et al.; A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 453; 2; 9-2006; 197-2060003-9861CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0003986106002451info:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2006.06.024info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:35:20Zoai:ri.conicet.gov.ar:11336/248325instacron: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:34982025-09-29 09:35:20.848CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
title A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
spellingShingle A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
Ferreyra, Raul Gabriel
Yeast
Sterol carrier protein
Yarrowia lipolytica
title_short A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
title_full A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
title_fullStr A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
title_full_unstemmed A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
title_sort A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
dc.creator.none.fl_str_mv Ferreyra, Raul Gabriel
Burgardt, Noelia Ines
Milikowski, Daniel
Melen, Gustavo
Kornblihtt, Alberto Rodolfo
Dell Angelica, Esteban
Santomé, José A.
Ermacora, Mario Roberto
author Ferreyra, Raul Gabriel
author_facet Ferreyra, Raul Gabriel
Burgardt, Noelia Ines
Milikowski, Daniel
Melen, Gustavo
Kornblihtt, Alberto Rodolfo
Dell Angelica, Esteban
Santomé, José A.
Ermacora, Mario Roberto
author_role author
author2 Burgardt, Noelia Ines
Milikowski, Daniel
Melen, Gustavo
Kornblihtt, Alberto Rodolfo
Dell Angelica, Esteban
Santomé, José A.
Ermacora, Mario Roberto
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Yeast
Sterol carrier protein
Yarrowia lipolytica
topic Yeast
Sterol carrier protein
Yarrowia lipolytica
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 14-kDa sterol carrier protein 2 (SCP2) domain is present in Eukaria, Bacteria and Archaea, and has been implicated in the transport and metabolism of lipids. We report the cloning, expression, purification and physicochemical characterization of a SCP2 from the yeast Yarrowia lipolytica (YLSCP2). Analytical size-exclusion chromatography, circular dichroism and fluorescence spectra, indicate that recombinant YLSCP2 is a well-folded monomer. Thermal unfolding experiments show that SCP2 maximal stability is at pH 7.0–9.0. YLSCP2 binds cis-parinaric acid and palmitoyl-CoA with KD values of 81 ± 40 nM and 73 ± 33 nM, respectively, sustaining for the first time the binding of fatty acids and their CoA esters to a nonanimal SCP2. The role of yeast SCP2 and other lipid binding proteins in transport, storage and peroxisomal oxidation of fatty acids is discussed.
Fil: Ferreyra, Raul Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Burgardt, Noelia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Milikowski, Daniel. Universidad Nacional de Quilmes; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Melen, Gustavo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Kornblihtt, Alberto Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Dell Angelica, Esteban. University of California at Los Angeles; Estados Unidos
Fil: Santomé, José A.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes; Argentina
description The 14-kDa sterol carrier protein 2 (SCP2) domain is present in Eukaria, Bacteria and Archaea, and has been implicated in the transport and metabolism of lipids. We report the cloning, expression, purification and physicochemical characterization of a SCP2 from the yeast Yarrowia lipolytica (YLSCP2). Analytical size-exclusion chromatography, circular dichroism and fluorescence spectra, indicate that recombinant YLSCP2 is a well-folded monomer. Thermal unfolding experiments show that SCP2 maximal stability is at pH 7.0–9.0. YLSCP2 binds cis-parinaric acid and palmitoyl-CoA with KD values of 81 ± 40 nM and 73 ± 33 nM, respectively, sustaining for the first time the binding of fatty acids and their CoA esters to a nonanimal SCP2. The role of yeast SCP2 and other lipid binding proteins in transport, storage and peroxisomal oxidation of fatty acids is discussed.
publishDate 2006
dc.date.none.fl_str_mv 2006-09
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/11336/248325
Ferreyra, Raul Gabriel; Burgardt, Noelia Ines; Milikowski, Daniel; Melen, Gustavo; Kornblihtt, Alberto Rodolfo; et al.; A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 453; 2; 9-2006; 197-206
0003-9861
CONICET Digital
CONICET
url http://hdl.handle.net/11336/248325
identifier_str_mv Ferreyra, Raul Gabriel; Burgardt, Noelia Ines; Milikowski, Daniel; Melen, Gustavo; Kornblihtt, Alberto Rodolfo; et al.; A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 453; 2; 9-2006; 197-206
0003-9861
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.sciencedirect.com/science/article/pii/S0003986106002451
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2006.06.024
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
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc.
publisher.none.fl_str_mv Elsevier Science 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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