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Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates
Open accessPublished version of a preprint
Abstract
Class I glutaredoxins (GRXs) are nearly ubiquitous proteins that catalyse the glutathione (GSH)-dependent reduction of mainly glutathionylated substrates. In land plants, a third class of GRXs has evolved (class III). Class III GRXs regulate the activity of TGA transcription factors through yet unexplored mechanisms. Here we show that Arabidopsis thaliana class III GRX ROXY9 is inactive as an oxidoreductase on widely used model substrates. Glutathionylation of the active site cysteine, a prerequisite for enzymatic activity, occurs only under highly oxidizing conditions established by the GSH/glutathione disulfide (GSSG) redox couple, while class I GRXs are readily glutathionylated even at very negative GSH/GSSG redox potentials. Thus, structural alterations in the GSH binding site leading to an altered GSH binding mode likely explain the enzymatic inactivity of ROXY9. This might have evolved to avoid overlapping functions with class I GRXs and raises questions of whether ROXY9 regulates TGA substrates through redox regulation.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences
Perez-Riverol, Y., Bai, J., Bandla, C., García-Seisdedos, D., Hewapathirana, S., Kamatchinathan, S., Kundu, D. J., Prakash, A., Frericks-Zipper, A., Eisenacher, M., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1038 · Cited by 6,125
Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
Deponte, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.018 · Cited by 1,150
Hanson, G. T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R. A., Tsien, R. Y., & Remington, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312846200 · Cited by 988
Rouhier, N., Lemaire, S. D., & Jacquot, J. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.59.032607.092811 · Cited by 593
Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 582
Baculovirus expression system for heterologous multiprotein complexes
Berger, I., Fitzgerald, D. J., & Richmond, T. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1036 · Cited by 502
Holmgren, A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2275 · Cited by 477
Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464
Ndamukong, I., Al-Abdallat, A. M., Thurow, C., Fode, B., Zander, M., Weigel, R. R., & Gatz, C. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03039.x · Cited by 456
Self-citationÅslund, F., Berndt, K. D., & Holmgren, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30780 · Cited by 418
Quantification of thiols and disulfides
Winther, J. R., & Thorpe, C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.03.031 · Cited by 401
Shoot-to-root mobile polypeptides involved in systemic regulation of nitrogen acquisition
Ohkubo, Y., Tanaka, M., Tabata, R., Ogawa, M., & Matsubayashi, Y. (2017) · Nature Plants · doi:10.1038/nplants.2017.29 · Cited by 391
Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase
Gravina, S. A., & Mieyal, J. J. (1993) · Biochemistry · doi:10.1021/bi00064a021 · Cited by 306
Characterization of human glutaredoxin 2 as iron–sulfur protein: A possible role as redox sensor
Lillig, C. H., Berndt, C., Vergnolle, O., Lönn, M. E., Hudemann, C., Bill, E., & Holmgren, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500735102 · Cited by 295
Murmu, J., Bush, M. J., DeLong, C. M. O., Li, S., Xu, M., Khan, M., Malcolmson, C., Fobert, P. R., Zachgo, S., & Hepworth, S. R. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.159111 · Cited by 254
Plant glutaredoxins: still mysterious reducing systems
Rouhier, N., Gelhaye, É., & Jacquot, J. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-3410-y · Cited by 219
Rouhier, N., Unno, H., Bandyopadhyay, S., Masip, L., Kim, S., Hirasawa, M., Gualberto, J. M., Lattard, V., Kusunoki, M., Knaff, D. B., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702268104 · Cited by 200
Glutaredoxin: Discovery, redox defense and much more
Ogata, F. T., Branco, V., Vale, F. F., & Coppo, L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101975 · Cited by 196
Li, S., Lauri, A., Ziemann, M., Busch, A. E., Bhave, M. R., & Zachgo, S. (2009) · The Plant Cell · doi:10.1105/tpc.108.064477 · Cited by 193
Xing, S., Rosso, M. G., & Zachgo, S. (2005) · Development · doi:10.1242/dev.01725 · Cited by 191
Redox Regulation in Photosynthetic Organisms: Focus on Glutathionylation
Zaffagnini, M., Bedhomme, M., Marchand, C. H., Morisse, S., Trost, P., & Lemaire, S. D. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4255 · Cited by 187
Kojer, K., Bien, M., Gangel, H., Morgan, B., Dick, T. P., & Riemer, J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.165 · Cited by 185
Evolution and diversity of glutaredoxins in photosynthetic organisms
Couturier, J., Jacquot, J., & Rouhier, N. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0054-y · Cited by 170
Fernandes, A. P., Fladvad, M., Berndt, C., Andrésen, C., Lillig, C. H., Neubauer, P. B., Sunnerhagen, M., Holmgren, A., & Vlamis‐Gardikas, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500678200 · Cited by 155
The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?
Deponte, M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7123 · Cited by 154
Yang, Y., Jao, S., Nanduri, S., Starke, D. W., Mieyal, J. J., & Qin, J. (1998) · Biochemistry · doi:10.1021/bi9806504 · Cited by 153
The Yeast Glutaredoxins Are Active as Glutathione Peroxidases
Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., & Grant, C. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111686200 · Cited by 150
Glutaredoxins in Thiol/Disulfide Exchange
Lillig, C. H., & Berndt, C. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5007 · Cited by 145
Non‐reciprocal regulation of the redox state of the glutathione–glutaredoxin and thioredoxin systems
Trotter, E. W., & Grant, C. M. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor729 · Cited by 143
Bedhomme, M., Adamo, M., Marchand, C. H., Couturier, J., Rouhier, N., Lemaire, S. D., Zaffagnini, M., & Trost, P. (2012) · Biochemical Journal · doi:10.1042/bj20120505 · Cited by 142
Zaffagnini, M., Michelet, L., Massot, V., Trost, P., & Lemaire, S. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709567200 · Cited by 138
Biochemical Characterization of Yeast Mitochondrial Grx5 Monothiol Glutaredoxin
Tamarit, J., Bellı́, G., Cabiscol, E., Herrero, E., & Ros, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303477200 · Cited by 129
Gradia, S., Ishida, J. P., Tsai, M.-S., Jeans, C., Tainer, J. A., & Fuss, J. O. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.03.008 · Cited by 127
The roles of glutaredoxins ligating Fe–S clusters: Sensing, transfer or repair functions?
Couturier, J., Przybyla‐Toscano, J., Roret, T., Claude Didierjean, B., & Rouhier, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.018 · Cited by 126
Aller, I., Rouhier, N., & Meyer, A. J. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00506 · Cited by 122
Glutaredoxin catalysis requires two distinct glutathione interaction sites
Begas, P., Liedgens, L., Moseler, A., Meyer, A. J., & Deponte, M. (2017) · Nature Communications · doi:10.1038/ncomms14835 · Cited by 117
Couturier, J., Ströher, E., Albetel, A., Roret, T., Muthuramalingam, M., Tarrago, L., Seidel, T., Tsan, P., Jacquot, J., Johnson, M. K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228726 · Cited by 112
Yang, Y. F., & Wells, W. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98964-7 · Cited by 108
Functional Partnership of the Copper Export Machinery and Glutathione Balance in Human Cells
Hatori, Y., Clasen, S. J., Hasan, N. M., Barry, A. N., & Lutsenko, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.381178 · Cited by 107
Couturier, J., Koh, C. S., Zaffagnini, M., Winger, A. M., Gualberto, J. M., Corbier, C., Decottignies, P., Jacquot, J., Lemaire, S. D., Claude Didierjean, B., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807998200 · Cited by 98
Yang, R., Xu, F., Wang, Y. M., Zhong, W., Dong, L., Shi, Y., Tang, T., Sheng, H., Jackson, D. P., & Yang, F. (2021) · Nature Plants · doi:10.1038/s41477-021-01029-2 · Cited by 96
Thiotransferase in human red blood cells: kinetics and equilibrium
Mieyal, J. J., Starke, D. W., Gravina, S. A., & Hocevar, B. A. (1991) · Biochemistry · doi:10.1021/bi00100a023 · Cited by 93
Redox regulation by glutathione needs enzymes
Berndt, C., Lillig, C. H., & Flohé, L. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00168 · Cited by 87
Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins
Trnka, D., Engelke, A. D., Gellert, M., Moseler, A., Hossain, M. F., Lindenberg, T. T., Pedroletti, L., Odermatt, B., de Souza, J. V. B., Bronowska, A. K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17323-0 · Cited by 85
Björnberg, O., Østergaard, H., & Winther, J. R. (2006) · Biochemistry · doi:10.1021/bi0522495 · Cited by 79
Ceylan, S., Seidel, V., Ziebart, N., Berndt, C., Dirdjaja, N., & Krauth‐Siegel, R. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.165860 · Cited by 79
Glutaredoxin-3 from Escherichia coli
Åslund, F., Nordstrand, K., Berndt, K. D., Nikkola, M., Bergman, T., Ponstingl, H., Jörnvall, H., Otting, G., & Holmgren, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6736 · Cited by 74
Origin and Diversification of Land Plant CC-Type Glutaredoxins
Ziemann, M., Bhave, M. R., & Zachgo, S. (2009) · Genome Biology and Evolution · doi:10.1093/gbe/evp025 · Cited by 72
A Thiol-Disulfide Transhydrogenase from Yeast
Nagai, S., & Black, S. H. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93532-5 · Cited by 66
Li, N., Muthreich, M., Huang, L., Thurow, C., Sun, T., Zhang, Y., & Gatz, C. (2018) · New Phytologist · doi:10.1111/nph.15496 · Cited by 65
Self-citationBerndt, C., Schwenn, J. D., & Lillig, C. H. (2015) · Chemical Science · doi:10.1039/c5sc01501d · Cited by 59
Uhrig, J. F., Huang, L., Barghahn, S., Willmer, M., Thurow, C., & Gatz, C. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.11.001 · Cited by 59
Self-citationLiedgens, L., Zimmermann, J., Wäschenbach, L., Geissel, F., Laporte, H., Gohlke, H., Morgan, B., & Deponte, M. (2020) · Nature Communications · doi:10.1038/s41467-020-15441-3 · Cited by 56
Ukuwela, A. A., Bush, A. I., Wedd, A. G., & Xiao, Z. (2017) · Chemical Science · doi:10.1039/c7sc04416j · Cited by 55
Couturier, J., Claude Didierjean, B., Jacquot, J., & Rouhier, N. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.11.050 · Cited by 48
Couturier, J., Jacquot, J., & Rouhier, N. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00518 · Cited by 46
Begas, P., Staudacher, V., & Deponte, M. (2015) · Chemical Science · doi:10.1039/c5sc01051a · Cited by 40
Geissel, F., Lang, L., Husemann, B., Morgan, B., & Deponte, M. (2024) · Nature Communications · doi:10.1038/s41467-024-45808-9 · Cited by 37
One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx
Zimmermann, J., Oestreicher, J., Hess, S., Herrmann, J. M., Deponte, M., & Morgan, B. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101598 · Cited by 35
Kobayashi, R., Ohkubo, Y., Izumi, M., Ota, R., Yamada, K., Hayashi, Y., Yamashita, Y., Noda, S., Ogawa, M., & Matsubayashi, Y. (2024) · Nature Communications · doi:10.1038/s41467-024-51091-5 · Cited by 34
Prescher, N., Hänsch, S., Knobbe-Thomsen, C. B., Stühler, K., & Poschmann, G. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.038 · Cited by 24
Self-citationZhao, H., Zhang, Y., Pan, M., Song, Y., Bai, L., Miao, Y., Huang, Y., Zhu, X., & Song, C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007557 · Cited by 23
Zannini, F., Moseler, A., Bchini, R., Dhalleine, T., Meyer, A. J., Rouhier, N., & Couturier, J. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.11.014 · Cited by 22
Manta, B., Möller, M. N., Bonilla, M., Deambrosi, M., Grunberg, K., Bellanda, M., Comini, M. A., & Ferrer‐Sueta, G. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006366 · Cited by 19
Schlößer, M., Moseler, A., Bodnar, Y., Homagk, M., Wagner, S., Pedroletti, L., Gellert, M., Ugalde, J. M., Lillig, C. H., & Meyer, A. J. (2024) · The Plant Journal · doi:10.1111/tpj.16687 · Cited by 15
Xu, H., Li, Z., Jiang, P., Zhao, L., Qu, C., de Peer, Y. V., Liu, Y., & Zeng, Q. (2022) · The Plant Journal · doi:10.1111/tpj.15660 · Cited by 14
In Vitro Alkylation Methods for Assessing the Protein Redox State
Zannini, F., Couturier, J., Keech, O., & Rouhier, N. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7225-8_4 · Cited by 14
Roret, T., Zhang, B., Moseler, A., Dhalleine, T., Gao, X., Couturier, J., Lemaire, S. D., Claude Didierjean, B., Johnson, M. K., & Rouhier, N. (2021) · Antioxidants · doi:10.3390/antiox10050803 · Cited by 6
Flagged first, then by citations
2 of the 71 references couldn’t be matched to a known paper.
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Sorted by citations
Schlößer, M., Moseler, A., Bodnar, Y., Homagk, M., Wagner, S., Pedroletti, L., Gellert, M., Ugalde, J. M., Lillig, C. H., & Meyer, A. J. (2024) · The Plant Journal · doi:10.1111/tpj.16687 · Cited by 15
Genetically encoded biosensors as gateways to retrograde redox signalling in live plants
Ugalde, J. M., & Meyer, A. J. (2025) · Journal of Experimental Botany · doi:10.1093/jxb/eraf080 · Cited by 12
Baidouri, M. E., Reichheld, J., & Belin, C. (2024) · Journal of Experimental Botany · doi:10.1093/jxb/erae232 · Cited by 11
Thurow, C., Pelizaeus, A. M., Mrozek, P. M., Hoßbach, B. M., Budimir, J., Schmitt, K., Valerius, O., Braus, G. H., & Gatz, C. (2025) · The Plant Cell · doi:10.1093/plcell/koaf038 · Cited by 10
Self-citationDugout, N., Martin, A., & Bach, L. (2025) · Plant and Soil · doi:10.1007/s11104-025-07593-2 · Cited by 5
Liu, J., Li, R., Xiang, M., Yuan, X., Tian, Y., Zhang, X., Wang, J., Wu, J., Zeng, Q., & Han, D. (2025) · Plant Science · doi:10.1016/j.plantsci.2025.112758 · Cited by 4
Lang, L., Diaz, C., Matonia, E., & Deponte, M. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104149 · Cited by 2
Yeom, W. W., Hong, J. K., Park, S. R., Lee, J., Suh, E.-J., Lee, S.-K., & Son, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148637 · Cited by 1
Xue, H., Li, Y., Xiao, J., Lu, Y., Xiang, Z., Hou, Z., Zhou, Y., & Tang, Q. (2026) · BMC Plant Biology · doi:10.1186/s12870-026-08207-4 · Cited by 1
Zhao, D., Huang, F., Zhang, H., Xie, Y., Bi, G., Liu, W., Han, Y., Chen, J., Zheng, Y., Wu, F., et al. (2026) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2026.07.011 · Cited by 1
Liu, X., Zhang, T., Quan, H., Li, Q., Wang, Z., Wang, D., Zhang, G., Zhang, H., Wang, X., & Yu, L. (2026) · Frontiers in Plant Science · doi:10.3389/fpls.2026.1826022 · Cited by 1
The Regulatory Functions of Thiol-Based Redoxins in Plant Cellular Physiology
Bae, S. B., Chae, H. B., Paeng, S. K., Wi, S. D., Kim, M. G., Cha, J., Jin, S., Zhao, M., & Lee, S. Y. (2026) · Journal of Plant Growth Regulation · doi:10.1007/s00344-026-12053-x
Ramos-Tamayo, C. C., Peralta-Castro, A., Guerrero-Largo, H., Ramos‐Pulido, J., Brieba, L. G., de Folter, S., & Marsch‐Martínez, N. (2026) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2026.111224
Molecular Analysis of Two CC-Type Glutaredoxins from the Model Legume Lotus japonicus
García-Díaz, I., Dı́az-Quintana, A., Roldán, M., Gómez‐Villegas, P., López‐Maury, L., García‐Calderón, M., Márquez, A. J., & Betti, M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27156703
Jin, K., Wang, Y., Bimpong, D., Chen, W., Chen, X., 王再岭, Wang, F., Gong, P., Yan, P., & Ma, D. M. (2026) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2026.111770
Metadata
- Authors
- Mrozek, P., Grunewald, S., Treffon, K., Poschmann, G., Rabe von Pappenheim, F., Tittmann, K., & Gatz, C.
- Affiliations
- University of Göttingen (DE)
- Düsseldorf University Hospital (DE)
- Max Planck Institute for Multidisciplinary Sciences (DE)
- Corresponding author
- Gatz, Christiane
- ORCID
- Venue
- Nature Communications
- Published
- 2025-01-11
- Volume
- 16
- Issue
- 1
- Pages
- 589-589
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11724882
- OpenAlex
- W4406274885
- Cited by
- 15
- References
- 71
- Citations by year
- 2026: 8 · 2025: 5
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (publishedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Deutsche Forschungsgemeinschaft (GA330/25, GA330/27)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- glutathionylation, oxidoreductase activity, TGA transcription factors, redox regulation, Arabidopsis thaliana, land plant evolution
- MeSH terms
- Cysteine, Glutathione, Oxidation-Reduction, Substrate Specificity, Arabidopsis, Glutathione Disulfide, Catalytic Domain, Arabidopsis Proteins, Glutaredoxins
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