Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins

Couturier J, Stroeher E, Albetel A-N, Roret T, Muthuramalingam M, Tarrago L, Seidel T, Tsan P, Jacquot J-P, Johnson MK, Dietz K-J, et al. (2011)
Journal of Biological Chemistry 286(31): 27515-27527.

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Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides (i.e. protein-glutathione adducts), and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, was shown to be localized in chloroplasts. A comparison of the biochemical, structural, and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicated that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the x-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys(32)) is required for cluster formation. In addition, thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter-or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism.
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Couturier J, Stroeher E, Albetel A-N, et al. Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry. 2011;286(31):27515-27527.
Couturier, J., Stroeher, E., Albetel, A. - N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., et al. (2011). Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry, 286(31), 27515-27527. doi:10.1074/jbc.M111.228726
Couturier, J., Stroeher, E., Albetel, A. - N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J. - P., Johnson, M. K., et al. (2011). Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry 286, 27515-27527.
Couturier, J., et al., 2011. Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry, 286(31), p 27515-27527.
J. Couturier, et al., “Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins”, Journal of Biological Chemistry, vol. 286, 2011, pp. 27515-27527.
Couturier, J., Stroeher, E., Albetel, A.-N., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J.-P., Johnson, M.K., Dietz, K.-J., Didierjean, C., Rouhier, N.: Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins. Journal of Biological Chemistry. 286, 27515-27527 (2011).
Couturier, Jeremy, Stroeher, Elke, Albetel, Angela-Nadia, Roret, Thomas, Muthuramalingam, Meenakumari, Tarrago, Lionel, Seidel, Thorsten, Tsan, Pascale, Jacquot, Jean-Pierre, Johnson, Michael K., Dietz, Karl-Josef, Didierjean, Claude, and Rouhier, Nicolas. “Arabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into Glutaredoxins”. Journal of Biological Chemistry 286.31 (2011): 27515-27527.
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PMID: 22891731
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Laporte D, Olate E, Salinas P, Salazar M, Jordana X, Holuigue L., J Exp Bot 63(1), 2012
PMID: 21963612
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PMID: 22288388
Protein-thiol oxidation and cell death: regulatory role of glutaredoxins.
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PMID: 22530666
Thioredoxin and glutaredoxin systems in plants: molecular mechanisms, crosstalks, and functional significance.
Meyer Y, Belin C, Delorme-Hinoux V, Reichheld JP, Riondet C., Antioxid Redox Signal 17(8), 2012
PMID: 22531002
Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro.
Bedhomme M, Adamo M, Marchand CH, Couturier J, Rouhier N, Lemaire SD, Zaffagnini M, Trost P., Biochem J 445(3), 2012
PMID: 22607208
Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.
Wang L, Ouyang B, Li Y, Feng Y, Jacquot JP, Rouhier N, Xia B., Protein Cell 3(9), 2012
PMID: 22886498
The biological roles of glutaredoxins.
Ströher E, Millar AH., Biochem J 446(3), 2012
PMID: 22928493
Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.
Couturier J, Vignols F, Jacquot JP, Rouhier N., FEBS Lett 586(21), 2012
PMID: 23022439

62 References

Data provided by Europe PubMed Central.

NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wuthrich K., Protein Sci. 1(3), 1992
PMID: 1304339
Glutaredoxins and thioredoxins in plants.
Meyer Y, Siala W, Bashandy T, Riondet C, Vignols F, Reichheld JP., Biochim. Biophys. Acta 1783(4), 2008
PMID: 18047840
Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: kinetics and specificity in deglutathionylation reactions.
Gao XH, Zaffagnini M, Bedhomme M, Michelet L, Cassier-Chauvat C, Decottignies P, Lemaire SD., FEBS Lett. 584(11), 2010
PMID: 20406640
In vivo targets of S-thiolation in Chlamydomonas reinhardtii.
Michelet L, Zaffagnini M, Vanacker H, Le Marechal P, Marchand C, Schroda M, Lemaire SD, Decottignies P., J. Biol. Chem. 283(31), 2008
PMID: 18534986
Glutaredoxins: roles in iron homeostasis.
Rouhier N, Couturier J, Johnson MK, Jacquot JP., Trends Biochem. Sci. 35(1), 2010
PMID: 19811920
How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
Berndt C, Hudemann C, Hanschmann EM, Axelsson R, Holmgren A, Lillig CH., Antioxid. Redox Signal. 9(1), 2007
PMID: 17115894
The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.
Ceylan S, Seidel V, Ziebart N, Berndt C, Dirdjaja N, Krauth-Siegel RL., J. Biol. Chem. 285(45), 2010
PMID: 20826822
Structural aspects of the distinct biochemical properties of glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae.
Discola KF, de Oliveira MA, Rosa Cussiol JR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimaraes BG, Netto LE., J. Mol. Biol. 385(3), 2009
PMID: 18992757

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