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Protein Science, Vol 7, Issue 12 2675-2680, Copyright © 1998 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Ca(2+)-dependent conformational changes in bovine GCAP-2

R. E. HUGHES, P. S. BRZOVIC, A. M. DIZHOOR, R. E. KLEVIT and J. B. HURLEY
Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195 Present address: Department of Genetics, University of Washington, Seattle, Washington 98195.

GCAP-2, a mammalian photoreceptor-specific protein, is a Ca(2+)-dependent regulator of the retinal membrane guanylyl cyclases (Ret-GCs). Sensing the fall in intracellular free Ca(2+) after photo-excitation, GCAP-2 stimulates the activity of Ret-GC leading to cGMP production. Like other members of the recoverin superfamily, GCAP-2 is a small N-myristoylated protein containing four EF-hand consensus motifs. In this study, we demonstrate that like recoverin and neurocalcin, GCAP-2 alters its conformation in response to Ca(2+)-binding as measured by a Ca(2+)-dependent change in its far UV CD spectrum. Differences in the conformation of the Ca(2+)-bound and Ca(2+)-free forms of GCAP-2 were also observed by examining their relative susceptibility to V8 protease. In contrast to recoverin, we do not observe proteolytic cleavage of the myristoylated N-terminus of Ca(2+)-bound GCAP-2. NMR spectra also show that, in contrast to recoverin, the chemical environment of the N-terminus of GCAP-2 is not dramatically altered by Ca(2+) binding. Despite the similarity of GCAP-2 and recoverin, the structural consequences of Ca(2+)-binding for these two proteins are significantly dissimilar.
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