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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/248325
Ver los metadatos del registro completo
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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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1844613099917672448 |
score |
13.070432 |