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Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway

(2016) PLANT PHYSIOLOGY. 172(2). p.858-873
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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.
Keywords
TANDEM AFFINITY PURIFICATION, PROTEIN INTERACTION NETWORK, WOBBLE, URIDINE MODIFICATION, TRANSFER-RNA, ARABIDOPSIS-THALIANA, SACCHAROMYCES-CEREVISIAE, MONOTHIOL GLUTAREDOXINS, ELONGATOR COMPLEX, GENE-EXPRESSION, CELL-CYCLE

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MLA
Iñigo, Sabrina, et al. “Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.” PLANT PHYSIOLOGY, vol. 172, no. 2, 2016, pp. 858–73, doi:10.1104/pp.16.00261.
APA
Iñigo, S., Nagels Durand, A., Ritter Traub, A., Le Gall, S., Termathe, M., Klassen, R., … Goossens, A. (2016). Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway. PLANT PHYSIOLOGY, 172(2), 858–873. https://doi.org/10.1104/pp.16.00261
Chicago author-date
Iñigo, Sabrina, Astrid Nagels Durand, Andrés Ritter Traub, Sabine Le Gall, Martin Termathe, Roland Klassen, Takayuki Tohge, et al. 2016. “Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.” PLANT PHYSIOLOGY 172 (2): 858–73. https://doi.org/10.1104/pp.16.00261.
Chicago author-date (all authors)
Iñigo, Sabrina, Astrid Nagels Durand, Andrés Ritter Traub, Sabine Le Gall, Martin Termathe, Roland Klassen, Takayuki Tohge, Barbara De Coninck, Jelle Van Leene, Rebecca De Clercq, Bruno PA Cammue, Alisdair R Fernie, Kris Gevaert, Geert De Jaeger, Sebastian A Leidel, Raffael Schaffrath, Maria Van Lijsebettens, Laurens Pauwels, and Alain Goossens. 2016. “Glutaredoxin GRXS17 Associates with the Cytosolic Iron-Sulfur Cluster Assembly Pathway.” PLANT PHYSIOLOGY 172 (2): 858–873. doi:10.1104/pp.16.00261.
Vancouver
1.
Iñigo S, Nagels Durand A, Ritter Traub A, Le Gall S, Termathe M, Klassen R, et al. Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway. PLANT PHYSIOLOGY. 2016;172(2):858–73.
IEEE
[1]
S. Iñigo et al., “Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway,” PLANT PHYSIOLOGY, vol. 172, no. 2, pp. 858–873, 2016.
@article{8510555,
  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.}},
  author       = {{Iñigo, Sabrina and Nagels Durand, Astrid and Ritter Traub, Andrés and Le Gall, Sabine and Termathe, Martin and Klassen, Roland and Tohge, Takayuki and De Coninck, Barbara and Van Leene, Jelle and De Clercq, Rebecca and Cammue, Bruno PA and Fernie, Alisdair R and Gevaert, Kris and De Jaeger, Geert and Leidel, Sebastian A and Schaffrath, Raffael and Van Lijsebettens, Maria and Pauwels, Laurens and Goossens, Alain}},
  issn         = {{0032-0889}},
  journal      = {{PLANT PHYSIOLOGY}},
  keywords     = {{TANDEM AFFINITY PURIFICATION,PROTEIN INTERACTION NETWORK,WOBBLE,URIDINE MODIFICATION,TRANSFER-RNA,ARABIDOPSIS-THALIANA,SACCHAROMYCES-CEREVISIAE,MONOTHIOL GLUTAREDOXINS,ELONGATOR COMPLEX,GENE-EXPRESSION,CELL-CYCLE}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{858--873}},
  title        = {{Glutaredoxin GRXS17 associates with the cytosolic iron-sulfur cluster assembly pathway}},
  url          = {{http://doi.org/10.1104/pp.16.00261}},
  volume       = {{172}},
  year         = {{2016}},
}

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