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  • Title: Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction.
    Author: Dizhoor AM, Chen CK, Olshevskaya E, Sinelnikova VV, Phillipov P, Hurley JB.
    Journal: Science; 1993 Feb 05; 259(5096):829-32. PubMed ID: 8430337.
    Abstract:
    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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