KORNBLIHTT Alberto Rodolfo
A yeast sterol carrier protein with fatty-acid and fatty-acyl-CoA binding activity
FERREYRA, R; BURGARDT, N; MILIKOWSKI, D; MELEN, G; KORNBLIHTT, A; DELL' ANGELICA, E; SANTOME, J; ERMACORA, M
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Año: 2006 vol. 453 p. 197 - 197
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 7.09.0. 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.