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Papers In Press, published online ahead of print May 31, 2000
Department of Physiology and Pharmacology, Texas A & M University, College Station, TX 77843-4466
Corresponding Author: fschroeder{at}cvm.tamu.edu
Although the 20 amino acid presequence present in 15 kDa pro-sterol carrier protein-2 (pro-SCP-2, the precursor of the mature 13 kDa SCP-2) alters the function of SCP-2 in lipid metabolism, the molecular basis for this effect is unresolved. The presequence dramatically altered SCP-2 structure as determined by circular dichroism, mass spectroscopy, and antibody accessibility such that pro-SCP-2 had 3-fold less -helix, 7-fold more -structure, 6-fold more reactive C-terminus to carboxypeptidase A, 2-fold less binding of anti-SCP-2, and did not enhance sterol transfer from plasma membranes. These differences were not due to protein stability since (i) the same concentration of guanidine hydrochloride was required for 50% unfolding, and (ii) the ligand binding sites displayed the same high affinity (nM Kds) in the order: cholesterol >> straight chain fatty acid > kinked chain fatty acid. Laser scanning confocal microscopy and double immunofluorescence demonstrated that pro-SCP-2 was more efficiently targeted to peroxisomes. Transfection of L-cells or McAR7777 hepatoma cells with cDNA encoding pro-SCP-2 resulted in 31% and 37% of SCP-2, respectively, colocalizing with the peroxisomal marker PMP70. In contrast, L-cells transfected with cDNA encoding SCP-2 exhibited 3-fold lower colocalization of SCP-2 with PMP70. In summary, the data suggest for the first time that the 20 amino acid presequence of pro-SCP-2 alters SCP-2 structure to facilitate peroxisomal targeting mediated by the C-terminal SKL peroxisomal targeting sequence.
J. Biol. Chem, 10.1074/jbc.M000431200
Submitted on January 18, 2000
Revised on May 25, 2000
Accepted on May 31, 2000
Pro-sterol carrier protein-2: Role of the N-terminal presequence in structure,function, and peroxisomal targeting
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