Abstract
KCNE1 (minK) is a membrane protein known to modulate the function of the KCNQ1 voltage-gated potassium ion channel in the human heart. KCNE1 has been over expressed and purified into SDS detergent and reconstituted into POPC/POPG lipid vesicles. We show that that KCNE1 maintains its ability to associate with and modulate KCNQ1 K+ channel activity when placed into POPC/POPG liposomes. Functional measurements of KCNE1 proteoliposomes were performed in Xenopus oocytes expressing KCNQ1 (KV7.1). Our CD measurements show that KCNE1 undergoes a global change in secondary structure when removed from a micelle environment and placed in a lipid bilayer. CW-EPR and Power Saturation EPR experiments have been used to examine the structural and dynamic properties of KCNE1 in micelles and lipid bilayer vesicles. The results indicate that KCNE1 inserts into the POPC/POPG vesicles, S28C and R32C are solvent-exposed and located outside the membrane, and S64C and F54C are buried inside the POPC/POPG lipid bilayer. The differences of KCNE1 placed into either micelles or lipid bilayers will be discussed.
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