Journal article
Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway



Publication Details
Authors:
Inigo, S.; Durand, A.; Ritter, A.; Le Gall, S.; Termathe, M.; Klassen, R.; Tohge, T.; De Coninck, B.; Van Leene, J.; De Clercq, R.; Cammue, B.; Fernie, A.; Gevaert, K.; De Jaeger, G.; Leidel, S.; Schaffrath, R.; Van Lijsebettens, M.; Pauwels, L.; Goossens, A.
Publisher:
AMER SOC PLANT BIOLOGISTS
Publication year:
2016
Journal:
Plant Physiology
Pages range:
858-873
Volume number:
172
Issue number:
2
Start page:
858
End page:
873
Number of pages:
16
ISSN:
0032-0889

Abstract
Cytosolic monothiol glutaredoxins (GRXs) are required in iron-sulfur (Fe-S) cluster delivery and iron sensing in yeast and mammals. In plants, it is unclear whether they have similar functions. Arabidopsis (Arabidopsis thaliana) has a sole class II cytosolic monothiol GRX encoded by GRXS17. Here, we used tandem affinity purification to establish that Arabidopsis GRXS17 associates with most known cytosolic Fe-S assembly (CIA) components. Similar to mutant plants with defective CIA components, grxs17 loss-of-function mutants showed some degree of hypersensitivity to DNA damage and elevated expression of DNA damage marker genes. We also found that several putative Fe-S client proteins directly bind to GRXS17, such as XANTHINE DEHYDROGENASE1 (XDH1), involved in the purine salvage pathway, and CYTOSOLIC THIOURIDYLASE SUBUNIT1 and CYTOSOLIC THIOURIDYLASE SUBUNIT2, both essential for the 2-thiolation step of 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) modification of tRNAs. Correspondingly, profiling of the grxs17-1 mutant pointed to a perturbed flux through the purine degradation pathway and revealed that it phenocopied mutants in the elongator subunit ELO3, essential for the mcm5 tRNA modification step, although we did not find XDH1 activity or tRNA thiolation to be markedly reduced in the grxs17-1 mutant. Taken together, our data suggest that plant cytosolic monothiol GRXs associate with the CIA complex, as in other eukaryotes, and contribute to, but are not essential for, the correct functioning of client Fe-S proteins in unchallenged conditions.


Authors/Editors

Last updated on 2019-25-07 at 18:59