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Defining the mechanism of the mitochondrial Atm1p [2Fe–2S] cluster exporter

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Abstract

Iron–sulfur cluster proteins play key roles in a multitude of physiological processes; including gene expression, nitrogen and oxygen sensing, electron transfer, and DNA repair. Biosynthesis of iron–sulfur clusters occurs in mitochondria on iron–sulfur cluster scaffold proteins in the form of [2Fe–2S] cores that are then transferred to apo targets within metabolic or respiratory pathways. The mechanism by which cytosolic Fe–S cluster proteins mature to their holo forms remains controversial. The mitochondrial inner membrane protein Atm1p can transport glutathione-coordinated iron–sulfur clusters, which may connect the mitochondrial and cytosolic iron–sulfur cluster assembly systems. Herein we describe experiments on the yeast Atm1p/ABCB7 exporter that provide additional support for a glutathione-complexed cluster as the natural physiological substrate and a reflection of the endosymbiotic model of mitochondrial evolution. These studies provide insight on the mechanism of cluster transport and the molecular basis of human disease conditions related to ABCB7. Recruitment of MgATP following cluster binding promotes a structural transition from closed to open conformations that is mediated by coupling helices, with MgATP hydrolysis facilitating the return to the closed state.

Graphical abstract: Defining the mechanism of the mitochondrial Atm1p [2Fe–2S] cluster exporter

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Supplementary files

Article information


Submitted
19 Nov 2019
Accepted
09 Apr 2020
First published
09 Apr 2020

Metallomics, 2020, Advance Article
Article type
Paper

Defining the mechanism of the mitochondrial Atm1p [2Fe–2S] cluster exporter

S. A. Pearson, C. Wachnowsky and J. A. Cowan, Metallomics, 2020, Advance Article , DOI: 10.1039/C9MT00286C

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