A novel mitochondrial carrier protein Mme1 acts as a yeast mitochondrial magnesium exporter

Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology submitted time 2016-05-12

Cui, Yixian Zhao, Shanke Wang, Juan Wang, Xudong Fan, Qiangwang Zhou, Bing Gao, Bingquan Sun, Fei

Abstract： The homeostasis of magnesium (Mg2+), an abundant divalent cation indispensable for many biological processes including mitochondrial functions, is underexplored. Previously, two mitochondrial Mg2+ importers, Mrs2 and Lpe10, were characterized for mitochondrial Mg2+ uptake. We now show that mitochondrial Mg2+ homeostasis is accurately controlled through the combined effects of previously known importers and a novel exporter, Mme1 (mitochondrial magnesium exporter 1). Mme1 belongs to the mitochondrial carrier family and was isolated for its mutation that is able to suppress the mrs2 Delta respiration defect. Deletion of MME1 significantly increased steady-state mitochondrial Mg2+ concentration, while overexpression decreased it. Measurements of Mg2+ exit from proteoliposomes reconstituted with purified Mme1 provided definite evidence for Mme1 as an Mg2+ exporter. Our studies identified, for the first time, a mitochondrial Mg2+ exporter that works together with mitochondrial importers to ensure the precise control of mitochondrial Mg2+ homeostasis. (C) 2015 Elsevier B.V. All rights reserved.

Peer Review Status:Awaiting Review

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