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)...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Milikowski, Daniel, Melen, Gustavo Javier, Kornblihtt, Alberto Rodolfo
Publicado: 2006
Materias:
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
Acyl-CoA Dehydrogenase
Amino Acid Sequence
Binding Sites
Carrier Proteins
Computer Simulation
Fatty Acids
Models, Chemical
Models, Molecular
Molecular Sequence Data
Protein Binding
Yarrowia
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v453_n2_p197_Ferreyra
http://hdl.handle.net/20.500.12110/paper_00039861_v453_n2_p197_Ferreyra
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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.

Ejemplares similares