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Protein Science, Vol 7, Issue 1 211-215, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Cloning, overexpression, purification, and spectroscopic characterization of human S100P

A. GRIBENKO, M. M. LOPEZ, J. M. RICHARDSON-III and G. I. MAKHATADZE
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061

The calcium-binding protein S100P has been found to be associated with human prostate cancer. We have overexpressed S100P in Escherichia coli using a T7 expression system. A rapid two-step procedure for the isolation of overexpressed S100P leads to a preparation of >95% pure protein with a yield of ~150 mg per liter of culture. The structural integrity of recombinant S100P was analyzed using CD and fluorescence spectroscopic techniques. The far-UV CD shows that secondary structure of recombinant S100P consists predominantly of {alpha}-helical structure. Both near-UV CD and tyrosine fluorescence spectra show that aromatic residues are involved in the formation of a specific, well packed structure, indicating that the recombinant S100P protein adopts a compact folded conformation. Ca(2+) has a profound effect on S100P structure. Near-UV CD and fluorescence intensity of both internal (tyrosine) and external (ANS) probes suggest significant structural rearrangements in the tertiary structure of the molecule. The similarity of far-UV CD spectrum of S100P in the presence and in the absence of Ca(2+) suggests that Ca(2+) binding has only minor effects on secondary structure.
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