S-nitrosylation: An emerging post-translational protein modification in plants

Astier, Jérémy; Rasul, Sumaira; Koen, Emmanuel; Manzoor, Hamid; Besson-Bard, Angélique; Lamotte, Olivier; Jeandroz, Sylvain; Durner, Joerg; Lindermayr, Christian; Wendehenne, David

doi:10.1016/j.plantsci.2011.02.011

Cited by 157 publications

(103 citation statements)

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“…To recognize their versatility, these have been named moonlighting proteins (Jeffery, 1999;Huberts and van der Klei, 2010;Sirover, 2011) and different mechanisms were proposed for the control of their moonlighting activity, chiefly posttranslational modifications and protein-protein interactions (Moore, 2004). Several reviews, largely inspired by studies on the animal field, have recently proposed plant GAPDH as an example of a moonlighting protein and S-nitrosylation of its catalytic Cys as a possible means to control GAPDH moonlighting activities (Astier et al, 2011;Gaupels et al, 2011). However, despite a general interest in nonglycolytic roles of plant GAPDHs, few reports have experimentally addressed the topic.…”

Section: Discussionmentioning

confidence: 99%

“…Not surprisingly, several proteomic studies have recently reported that H 2 O 2 , NO-donors, and biotic and abiotic stresses applied to plants may affect the redox state of reactive protein cysteines, in addition to affecting their transcriptomic and proteomic profiles Polverari et al, 2003;Parani et al, 2004;Lindermayr et al, 2005;Herbette et al, 2006;Roth et al, 2006;Sarry et al, 2006;Besson-Bard et al, 2008;Romero-Puertas et al, 2008;Astier et al, 2011). Because of the high reactivity of its catalytic Cys, cytosolic glyceraldehyde 3-P dehydrogenase (GAPDH) has been identified as a target of different types of redox modifications (Hancock et al, 2005(Hancock et al, , 2006Lindermayr et al, 2005;Holtgrefe et al, 2008;Bedhomme et al, 2012).…”

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confidence: 99%

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Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

et al. 2013

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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in the glycolytic pathway. It has been widely demonstrated that mammalian GAPDH, in addition to its role in glycolysis, fulfills alternative functions mainly linked to its susceptibility to oxidative posttranslational modifications. Here, we investigated the responses of Arabidopsis (Arabidopsis thaliana) cytosolic GAPDH isoenzymes GAPC1 and GAPC2 to cadmium-induced stress in seedlings roots. GAPC1 was more responsive to cadmium than GAPC2 at the transcriptional level. In vivo, cadmium treatments induced different concomitant effects, including (1) nitric oxide accumulation, (2) cytosolic oxidation (e.g. oxidation of the redox-sensitive Green fluorescent protein2 probe), (3) activation of the GAPC1 promoter, (4) GAPC1 protein accumulation in enzymatically inactive form, and (5) strong relocalization of GAPC1 to the nucleus. All these effects were detected in the same zone of the root tip. In vitro, GAPC1 was inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition was directly provided by cadmium. Interestingly, nuclear relocalization of GAPC1 under cadmium-induced oxidative stress was stimulated, rather than inhibited, by mutating into serine the catalytic cysteine of GAPC1 (C155S), excluding an essential role of GAPC1 nitrosylation in the mechanism of nuclear relocalization, as found in mammalian cells. Although the function of GAPC1 in the nucleus is unknown, our results suggest that glycolytic GAPC1, through its high sensitivity to the cellular redox state, may play a role in oxidative stress signaling or protection in plants.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

et al. 2013

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“…In many biological systems, nitrosylation participates in signaling (reviewed in Astier et al, 2011Astier et al, , 2012 or induces protein degradation (Souza et al, 2000, Kim et al, 2004Lee et al, 2008;Wei et al, 2011;Tang et al, 2012;Jaba et al, 2013). Here, we reasoned that most of the cytochrome b 6 f subunits and biogenesis factors belong to heme binding complexes or participate in the biogenesis of heme binding proteins, which are particularly prone to nitrosylation (Thomas et al, 2003;Angelo et al, 2008).…”

Section: No Is Involved In the Remodeling Of Photosynthesis During Nimentioning

confidence: 99%

Nitric Oxide–Triggered Remodeling of Chloroplast Bioenergetics and Thylakoid Proteins upon Nitrogen Starvation inChlamydomonas reinhardtii

et al. 2014

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Starving microalgae for nitrogen sources is commonly used as a biotechnological tool to boost storage of reduced carbon into starch granules or lipid droplets, but the accompanying changes in bioenergetics have been little studied so far. Here, we report that the selective depletion of Rubisco and cytochrome b 6 f complex that occurs when Chlamydomonas reinhardtii is starved for nitrogen in the presence of acetate and under normoxic conditions is accompanied by a marked increase in chlororespiratory enzymes, which converts the photosynthetic thylakoid membrane into an intracellular matrix for oxidative catabolism of reductants. Cytochrome b 6 f subunits and most proteins specifically involved in their biogenesis are selectively degraded, mainly by the FtsH and Clp chloroplast proteases. This regulated degradation pathway does not require light, active photosynthesis, or state transitions but is prevented when respiration is impaired or under phototrophic conditions. We provide genetic and pharmacological evidence that NO production from intracellular nitrite governs this degradation pathway: Addition of a NO scavenger and of two distinct NO producers decrease and increase, respectively, the rate of cytochrome b 6 f degradation; NO-sensitive fluorescence probes, visualized by confocal microscopy, demonstrate that nitrogen-starved cells produce NO only when the cytochrome b 6 f degradation pathway is activated.

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“…Two recent reports also identified PGK from land plants as a putative target of nitrosylation (53,54). These additional redox post-translational modifications started to be recognized as important regulatory mechanisms involved in the control of numerous cellular plant processes under stress conditions (16,(55)(56)(57)(58). Further studies will therefore be required to determine whether chloroplastic PGK is tightly controlled by multiple redox-regulatory mechanisms, to analyze how the complex interplay between varying environmental conditions and the intracellular redox state determine the type and the extent of each redox modification and to understand how these mechanisms contribute to the fine tuning of carbon fixation in photosynthetic organisms.…”

Section: Conditionsmentioning

confidence: 99%

Thioredoxin-dependent Redox Regulation of Chloroplastic Phosphoglycerate Kinase from Chlamydomonas reinhardtii

Morisse

Michelet

Bedhomme

et al. 2014

Journal of Biological Chemistry

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Background: Chloroplastic PGK is a putative target of thioredoxin identified by redox proteomics. Results: Chlamydomonas PGK1 is regulated by TRX-f via oxidoreduction of the Cys 227 -Cys 361 disulfide bond. Conclusion: Chlamydomonas PGK1 is a potentially new light-modulated Calvin-Benson cycle enzyme. Significance: The complex redox regulation of the Calvin-Benson cycle and its evolution are further expanded.

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S-nitrosylation: An emerging post-translational protein modification in plants

Cited by 157 publications

References 59 publications

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

Nitric Oxide–Triggered Remodeling of Chloroplast Bioenergetics and Thylakoid Proteins upon Nitrogen Starvation inChlamydomonas reinhardtii

Thioredoxin-dependent Redox Regulation of Chloroplastic Phosphoglycerate Kinase from Chlamydomonas reinhardtii

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