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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kruse, Inga Schwarzländer, Markus Van Veen, Hendrik W. Balk, Janneke Thornton, Jeremy D. Meyer, Andreas J. Schaedler, Theresia A. |
| Description | Author Affiliation: Schaedler TA ( From the John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom, the Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, United Kingdom.); Thornton JD ( From the John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.); Kruse I ( From the John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom, the School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom.); Schwarzländer M ( the Institute of Crop Science and Resource Conservation, University of Bonn, 53113 Bonn, Germany.); Meyer AJ ( the Institute of Crop Science and Resource Conservation, University of Bonn, 53113 Bonn, Germany.); van Veen HW ( the Department of Pharmacology, University of Cambridge, Cambridge CB2 1PD, United Kingdom, and hwv20@cam.ac.uk.); Balk J ( From the John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom, the School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom janneke.balk@jic.ac.uk.) |
| Abstract | An ATP-binding cassette transporter located in the inner mitochondrial membrane is involved in iron-sulfur cluster and molybdenum cofactor assembly in the cytosol, but the transported substrate is unknown. ATM3 (ABCB25) from Arabidopsis thaliana and its functional orthologue Atm1 from Saccharomyces cerevisiae were expressed in Lactococcus lactis and studied in inside-out membrane vesicles and in purified form. Both proteins selectively transported glutathione disulfide (GSSG) but not reduced glutathione in agreement with a 3-fold stimulation of ATPase activity by GSSG. By contrast, $Fe^{2+}$ alone or in combination with glutathione did not stimulate ATPase activity. Arabidopsis atm3 mutants were hypersensitive to an inhibitor of glutathione biosynthesis and accumulated GSSG in the mitochondria. The growth phenotype of atm3-1 was strongly enhanced by depletion of the mitochondrion-localized, GSH-dependent persulfide oxygenase ETHE1, suggesting that the physiological substrate of ATM3 contains persulfide in addition to glutathione. Consistent with this idea, a transportomics approach using mass spectrometry showed that glutathione trisulfide (GS-S-SG) was transported by Atm1. We propose that mitochondria export glutathione polysulfide, containing glutathione and persulfide, for iron-sulfur cluster assembly in the cytosol. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 34 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-08-22 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | ATP-Binding Cassette Transporters Metabolism Arabidopsis Proteins Conserved Sequence Cytosol Glutathione Mitochondrial Proteins Physiology Saccharomyces Cerevisiae Proteins Sulfides Chemistry Genetics Adenosine Triphosphatases Amino Acid Sequence Arabidopsis Biological Transport Biosynthesis Molecular Sequence Data Saccharomyces Cerevisiae Sequence Homology, Amino Acid Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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