A. Frolov et al., STEROL CARRIER PROTEIN-2, A NEW FATTY ACYL-COENZYME A-BINDING PROTEIN, The Journal of biological chemistry, 271(50), 1996, pp. 31878-31884
The ability of sterol carrier protein-2 (SCP-2) to interact with long
chain fatty acyl-CoAs was examined. SCP-2 bound fluorescent fatty acyl
-CoAs at a single site with high affinity, K-d values for cis- and tra
ns-parinaroyl-CoA were 4.5 and 2.8 nM, respectively. Saturated 10-18-c
arbon and unsaturated 14-20-carbon fatty acyl-CoAs displaced SCP-2-bou
nd fluorescent ligand. Oleoyl-CoA and oleic acid (but not coenzyme A)
significantly altered SCP-2 Trp(50) emission and anisotropy decay, the
reby increasing SCP-2 rotational correlation time, SCP-2 hydrodynamic
radius, and SCP-2 Trp(50) remaining anisotropy up to 1.7-, 1.2-, and 1
.3-fold, respectively. These changes were not accompanied by significa
nt alterations in protein secondary structure as determined by circula
r dichroism, Finally, SCP-2 differentially altered the fluorescence em
ission and anisotropy decays of bound cis- and trans-parinaroyl-CoA. B
oth fluorescent fatty acyl-CoAs were located within a very ordered (li
mited cone angle of rotation) environment within SCP-2, as shown by a
remaining anisotropy of 0.365 and 0.361 and a wobbling cone angle of 1
2 and 13 degrees, respectively. These anisotropy values were very clos
e to those of such ligands in a propylene glass. However, the rotation
al relaxation times exhibited by SCP-2-bound cis- and trans-parinaroyl
-CoA, 8.4-8.8 ns, were longer than those for the corresponding free fa
tty acid, 7.5-6.6 ns. These data show for the first time that SCP-2 is
a fatty acyl-CoA-binding protein.