A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
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)...
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todo:paper_00039861_v453_n2_p197_Ferreyra2023-10-03T13:57:03Z A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity Ferreyra, R.G. Burgardt, N.I. Milikowski, D. Melen, G. Kornblihtt, A.R. Dell' Angelica, E.C. Santomé, J.A. Ermácora, M.R. Circular dichroism Fatty-acid Fatty-acyl-CoA Lipid binding protein Peroxisomes Sterol carrier protein Yarrowia lipolytica Yeast acyl coenzyme A fatty acid lipid lipid binding protein palmitoyl coenzyme A parinaric acid recombinant protein sterol carrier protein 2 article circular dichroism fatty acid oxidation fluorescence spectroscopy gel permeation chromatography molecular cloning nonhuman nucleotide sequence peroxisome priority journal protein domain protein expression protein folding protein function protein purification protein stability Yarrowia lipolytica Acyl-CoA Dehydrogenase Amino Acid Sequence Binding Sites Carrier Proteins Computer Simulation Fatty Acids Models, Chemical Models, Molecular Molecular Sequence Data Protein Binding Yarrowia Yarrowia lipolytica 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. © 2006 Elsevier Inc. All rights reserved. Fil:Milikowski, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Melen, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kornblihtt, A.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v453_n2_p197_Ferreyra |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Circular dichroism Fatty-acid Fatty-acyl-CoA Lipid binding protein Peroxisomes Sterol carrier protein Yarrowia lipolytica Yeast acyl coenzyme A fatty acid lipid lipid binding protein palmitoyl coenzyme A parinaric acid recombinant protein sterol carrier protein 2 article circular dichroism fatty acid oxidation fluorescence spectroscopy gel permeation chromatography molecular cloning nonhuman nucleotide sequence peroxisome priority journal protein domain protein expression protein folding protein function protein purification protein stability Yarrowia lipolytica Acyl-CoA Dehydrogenase Amino Acid Sequence Binding Sites Carrier Proteins Computer Simulation Fatty Acids Models, Chemical Models, Molecular Molecular Sequence Data Protein Binding Yarrowia Yarrowia lipolytica |
| spellingShingle |
Circular dichroism Fatty-acid Fatty-acyl-CoA Lipid binding protein Peroxisomes Sterol carrier protein Yarrowia lipolytica Yeast acyl coenzyme A fatty acid lipid lipid binding protein palmitoyl coenzyme A parinaric acid recombinant protein sterol carrier protein 2 article circular dichroism fatty acid oxidation fluorescence spectroscopy gel permeation chromatography molecular cloning nonhuman nucleotide sequence peroxisome priority journal protein domain protein expression protein folding protein function protein purification protein stability Yarrowia lipolytica Acyl-CoA Dehydrogenase Amino Acid Sequence Binding Sites Carrier Proteins Computer Simulation Fatty Acids Models, Chemical Models, Molecular Molecular Sequence Data Protein Binding Yarrowia Yarrowia lipolytica Ferreyra, R.G. Burgardt, N.I. Milikowski, D. Melen, G. Kornblihtt, A.R. Dell' Angelica, E.C. Santomé, J.A. Ermácora, M.R. A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity |
| topic_facet |
Circular dichroism Fatty-acid Fatty-acyl-CoA Lipid binding protein Peroxisomes Sterol carrier protein Yarrowia lipolytica Yeast acyl coenzyme A fatty acid lipid lipid binding protein palmitoyl coenzyme A parinaric acid recombinant protein sterol carrier protein 2 article circular dichroism fatty acid oxidation fluorescence spectroscopy gel permeation chromatography molecular cloning nonhuman nucleotide sequence peroxisome priority journal protein domain protein expression protein folding protein function protein purification protein stability Yarrowia lipolytica Acyl-CoA Dehydrogenase Amino Acid Sequence Binding Sites Carrier Proteins Computer Simulation Fatty Acids Models, Chemical Models, Molecular Molecular Sequence Data Protein Binding Yarrowia Yarrowia lipolytica |
| 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. © 2006 Elsevier Inc. All rights reserved. |
| format |
JOUR |
| author |
Ferreyra, R.G. Burgardt, N.I. Milikowski, D. Melen, G. Kornblihtt, A.R. Dell' Angelica, E.C. Santomé, J.A. Ermácora, M.R. |
| author_facet |
Ferreyra, R.G. Burgardt, N.I. Milikowski, D. Melen, G. Kornblihtt, A.R. Dell' Angelica, E.C. Santomé, J.A. Ermácora, M.R. |
| author_sort |
Ferreyra, R.G. |
| title |
A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity |
| 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 |
yeast sterol carrier protein with fatty-acid and fatty-acyl-coa binding activity |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v453_n2_p197_Ferreyra |
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