Journal
PLANT PHYSIOLOGY
Volume 184, Issue 2, Pages 676-692Publisher
OXFORD UNIV PRESS INC
DOI: 10.1104/pp.20.00906
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Funding
- Centre National de la Recherche Scientifique
- Agence Nationale de la Recherche [ANR-Cynthiol 12-BSV6-0011, ANR-REPHARE 19-CE12-0027, ANR-LABX-011, EQUIPEX CACSICE ANR-11-EQPX-0008]
- Proteomic Platform of IBPC (PPI)
- Labex AGRO (under I-Site Muse framework) [2016-03]
- Laboratoires d'Excellence TULIP [ANR-10-LABX-41]
- Universite de Perpignan Via Domitia [ED305]
- Research Foundation-Flanders (Excellence of Science) [30829584, G0D7914N]
- VUB Strategic Research Programme [SRP34]
- Deutsche Forschungsgemeinschaft [SCHE 217, SPP 1710, SFB 987]
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Heat stress induces misfolding and aggregation of proteins unless they are guarded by chaperone systems. Here, we examined the function of the glutaredoxin GRXS17, a member of thiol reductase families in the model plant Arabidopsis (Arabidopsis thaliana). GRXS17 is a nucleocytosolic monothiol glutaredoxin consisting of an N-terminal thioredoxin domain and three CGFS active-site motif-containing GRX domains that coordinate three iron-sulfur (Fe-S) clusters in a glutathione-dependent manner. As an Fe-S cluster-charged holoenzyme, GRXS17 is likely involved in the maturation of cytosolic and nuclear Fe-S proteins. In addition to its role in cluster biogenesis, GRXS17 presented both foldase and redox-dependent holdase activities. Oxidative stress in combination with heat stress induced loss of its Fe-S clusters followed by subsequent formation of disulfide bonds between conserved active-site cysteines in the corresponding thioredoxin domains. This oxidation led to a shift of GRXS17 to a high-molecular-weight complex and thus activated its holdase activity in vitro. Moreover, GRXS17 was specifically involved in plant tolerance to moderate high temperature and protected root meristematic cells from heat-induced cell death. Finally, GRXS17 interacted with a different set of proteins upon heat stress, possibly protecting them from heat injuries. Therefore, we propose that the Fe-S cluster enzyme GRXS17 is an essential guard that protects proteins against moderate heat stress, likely through a redox-dependent chaperone activity. We reveal the mechanism of an Fe-S cluster-dependent activity shift that converts the holoenzyme GRXS17 into a holdase, thereby preventing damage caused by heat stress.
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