Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel

Ming Li, Yang Li, Yue Lu, Jianhui Li, Xuhang Lu, Yue Ren, Tianlei Wen, Yaojie Wang, Shenghai Chang, Xing Zhang, Xue Yang () and Yuequan Shen ()
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Ming Li: Nankai University
Yang Li: Nankai University
Yue Lu: Nankai University
Jianhui Li: Nankai University
Xuhang Lu: Nankai University
Yue Ren: Nankai University
Tianlei Wen: Nankai University
Yaojie Wang: Nankai University
Shenghai Chang: Zhejiang University
Xing Zhang: Zhejiang University
Xue Yang: Nankai University
Yuequan Shen: Nankai University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Mitochondrial RNA splicing 2 (Mrs2), a eukaryotic CorA ortholog, enables Mg2+ to permeate the inner mitochondrial membrane and plays an important role in mitochondrial metabolic function. However, the mechanism by which Mrs2 permeates Mg2+ remains unclear. Here, we report four cryo-electron microscopy (cryo-EM) reconstructions of Homo sapiens Mrs2 (hMrs2) under various conditions. All of these hMrs2 structures form symmetrical pentamers with very similar pentamer and protomer conformations. A special structural feature of Cl−-bound R-ring, which consists of five Arg332 residues, was found in the hMrs2 structure. Molecular dynamics simulations and mitochondrial Mg2+ uptake assays show that the R-ring may function as a charge repulsion barrier, and Cl− may function as a ferry to jointly gate Mg2+ permeation in hMrs2. In addition, the membrane potential is likely to be the driving force for Mg2+ permeation. Our results provide insights into the channel assembly and Mg2+ permeation of hMrs2.

Date: 2023
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DOI: 10.1038/s41467-023-40516-2

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