Groningen Biomolecular & Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG, Groningen, the Netherlands.
Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Sci Rep. 2020 Jan 21;10(1):840. doi: 10.1038/s41598-020-57869-z.
CorA proteins belong to 2-TM-GxN family of membrane proteins, and play a major role in Mg transport in prokaryotes and eukaryotic mitochondria. The selection of substrate is believed to occur via the signature motif GxN, however there is no consensus how strict this selection within the family. To answer this question, we employed fluorescence-based transport assays on three different family members, namely CorA from bacterium Thermotoga maritima, CorA from the archeon Methanocaldococcus jannaschii and ZntB from bacterium Escherichia coli, reconstituted into proteoliposomes. Our results show that all three proteins readily transport Mg, Co, Ni and Zn, but not Al. Despite the similarity in cation specificity, ZntB differs from the CorA proteins, as in the former transport is stimulated by a proton gradient, but in the latter by the membrane potential, confirming the hypothesis that CorA and ZntB proteins diverged to different transport mechanisms within the same protein scaffold.
CorA 蛋白属于 2-TM-GxN 家族的膜蛋白,在原核生物和真核生物线粒体的 Mg 转运中发挥主要作用。据信,底物的选择是通过特征基序 GxN 发生的,但对于该家族内的这种选择有多严格尚无共识。为了回答这个问题,我们在三种不同的家族成员(即来自细菌 Thermotoga maritima 的 CorA、来自古菌 Methanocaldococcus jannaschii 的 CorA 和来自细菌 Escherichia coli 的 ZntB)上进行了基于荧光的转运测定,这些蛋白均被重构成了类脂体。我们的结果表明,所有三种蛋白都能轻易地转运 Mg、Co、Ni 和 Zn,但不能转运 Al。尽管阳离子特异性相似,但 ZntB 与 CorA 蛋白不同,因为在前一种蛋白中,转运是由质子梯度刺激的,但在后一种蛋白中,转运是由膜电位刺激的,这证实了 CorA 和 ZntB 蛋白在同一蛋白支架内分化为不同的转运机制的假设。