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). 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.
Ferreyra
Raúl G
RG
Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Argentina.
Burgardt
Noelia I
NI
Milikowski
Daniel
D
Melen
Gustavo
G
Kornblihtt
Alberto R
AR
Dell' Angelica
Esteban C
EC
Santomé
José A
JA
Ermácora
Mario R
MR
D042964:Acyl-CoA Dehydrogenase / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D003198:Computer Simulation; D005227:Fatty Acids / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D025062:Yarrowia / Q000378:metabolism*
D002352:Carrier Proteins; D005227:Fatty Acids; C072087:sterol carrier proteins; D042964:Acyl-CoA Dehydrogenase