期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 44, 页码 13735-13740出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1510835112
关键词
glutaredoxin; iron-sulfur cluster; mitochondria; aconitase; glutathione
资金
- Deutsche Forschungsgemeinschaft (DFG) [ME1567/5-1]
- priority program Dynamics of thiol-based redox switches in cellular physiology [DFG SPP1710, ME1567/9-1, BE3259/5-1]
- Emmy Noether Program Grant [SCHW1719/1-1]
- Ministry of Innovation, Science and Research within NRW Strategieprojekt BioSC [313/323-400-002 13]
The iron-sulfur cluster (ISC) is an ancient and essential cofactor of many proteins involved in electron transfer and metabolic reactions. In Arabidopsis, three pathways exist for the maturation of iron-sulfur proteins in the cytosol, plastids, and mitochondria. We functionally characterized the role of mitochondrial glutaredoxin S15 (GRXS15) in biogenesis of ISC containing aconitase through a combination of genetic, physiological, and biochemical approaches. Two Arabidopsis T-DNA insertion mutants were identified as null mutants with early embryonic lethal phenotypes that could be rescued by GRXS15. Furthermore, we showed that recombinant GRXS15 is able to coordinate and transfer an ISC and that this coordination depends on reduced glutathione (GSH). We found the Arabidopsis GRXS15 able to complement growth defects based on disturbed ISC protein assembly of a yeast Delta grx5 mutant. Modeling of GRXS15 onto the crystal structures of related nonplant proteins highlighted amino acid residues that after mutation diminished GSH and subsequently ISC coordination, as well as the ability to rescue the yeast mutant. When used for plant complementation, one of these mutant variants, GRXS15(K83/A), led to severe developmental delay and a pronounced decrease in aconitase activity by approximately 65%. These results indicate that mitochondrial GRXS15 is an essential protein in Arabidopsis, required for full activity of iron-sulfur proteins.
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