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Science 5 February 1993:
Vol. 259. no. 5096, pp. 829 - 832
DOI: 10.1126/science.8430337

Articles

Science, Vol 259, Issue 5096, 829-832
Copyright © 1993 by American Association for the Advancement of Science


articles

Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction

AM Dizhoor, CK Chen, E Olshevskaya, VV Sinelnikova, P Phillipov, and JB Hurley

Department of Biochemistry, University of Washington, Seattle 98195.

Recoverin, a calcium ion (Ca2+)-binding protein of vertebrate photoreceptors, binds to photoreceptor membranes when the Ca2+ concentration is greater than 1 micromolar. This interaction requires a fatty acyl residue covalently linked to the recoverin amino (NH2)-terminus. Removal of the acyl residue, either by proteolytic cleavage of the NH2-terminus or by production of nonacylated recoverin, prevented recoverin from binding to membranes. The acylated recoverin NH2-terminus could be cleaved by trypsin only when Ca2+ was bound to recoverin. These results suggest that the hydrophobic NH2-terminus is constrained in Ca(2+)-free recoverin and liberated by Ca2+ binding. The hydrophobic acyl moiety of recoverin may interact with the membrane only when recoverin binds Ca2+.


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