The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment

Chibani, Kamel; Couturier, Jérémy; Selles, Benjamin; Jacquot, Jean‐Pierre; Rouhier, Nicolas

doi:10.1007/s11120-009-9501-8

Cited by 30 publications

(19 citation statements)

References 164 publications

(193 reference statements)

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“…The modified redox status of the chloroplasts is instrumental in regulating the activity of numerous metabolic enzymes accordingly (14,68). Interestingly, this work now provides evidence for a post-translational, redoxdependent regulation of AtTPPD.…”

Section: Discussionmentioning

confidence: 65%

The Redox-Sensitive Chloroplast Trehalose-6-Phosphate Phosphatase AtTPPD Regulates Salt Stress Tolerance

Krasensky

Broyart

Rabanal

et al. 2014

Antioxidants & Redox Signaling

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Aims: High salinity stress impairs plant growth and development. Trehalose metabolism has been implicated in sugar signaling, and enhanced trehalose metabolism can positively regulate abiotic stress tolerance. However, the molecular mechanism(s) of the stress-related trehalose pathway and the role of individual trehalose biosynthetic enzymes for stress tolerance remain unclear. Results: Trehalose-6-phosphate phosphatase (TPP) catalyzes the final step of trehalose metabolism. Investigating the subcellular localization of the Arabidopsis thaliana TPP family members, we identified AtTPPD as a chloroplast-localized enzyme. Plants deficient in AtTPPD were hypersensitive, whereas plants overexpressing AtTPPD were more tolerant to high salinity stress. Elevated stress tolerance of AtTPPD overexpressors correlated with high starch levels and increased accumulation of soluble sugars, suggesting a role for AtTPPD in regulating sugar metabolism under salinity conditions. Biochemical analyses indicate that AtTPPD is a target of post-translational redox regulation and can be reversibly inactivated by oxidizing conditions. Two cysteine residues were identified as the redox-sensitive sites. Structural and mutation analyses suggest that the formation of an intramolecular disulfide bridge regulates AtTPPD activity. Innovation: The activity of different AtTPP isoforms, located in the cytosol, nucleus, and chloroplasts, can be redox regulated, suggesting that the trehalose metabolism might relay the redox status of different cellular compartments to regulate diverse biological processes such as stress responses. Conclusion: The evolutionary conservation of the two redox regulatory cysteine residues of TPPs in spermatophytes indicates that redox regulation of TPPs might be a common mechanism enabling plants to rapidly adjust trehalose metabolism to the prevailing environmental and developmental conditions. Antioxid. Redox Signal. 21, 1289-1304.

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Section: Discussionmentioning

confidence: 65%

The Redox-Sensitive Chloroplast Trehalose-6-Phosphate Phosphatase AtTPPD Regulates Salt Stress Tolerance

Krasensky

Broyart

Rabanal

et al. 2014

Antioxidants & Redox Signaling

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“…Redox state and GSH affect the function of many enzymes through post-translational modifications such as disulfide bond reduction and cysteine glutathionylation [53]. For instance, thioredoxins and glutaredoxins, which are involved in the formation/reduction of disulfide bonds between proteins, have been implicated in the regulation of chloroplast metabolism [54], [55]. ADP glucose pyrophosphorylase, a key enzyme in the biosynthesis of starch was also shown to be redox regulated [56], [57].…”

Section: Discussionmentioning

confidence: 99%

(Homo)glutathione Deficiency Impairs Root-knot Nematode Development in Medicago truncatula

Baldacci‐Cresp

Chang²,

Maucourt³

et al. 2012

PLoS Pathog

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Root-knot nematodes (RKN) are obligatory plant parasitic worms that establish and maintain an intimate relationship with their host plants. During a compatible interaction, RKN induce the redifferentiation of root cells into multinucleate and hypertrophied giant cells essential for nematode growth and reproduction. These metabolically active feeding cells constitute the exclusive source of nutrients for the nematode. Detailed analysis of glutathione (GSH) and homoglutathione (hGSH) metabolism demonstrated the importance of these compounds for the success of nematode infection in Medicago truncatula. We reported quantification of GSH and hGSH and gene expression analysis showing that (h)GSH metabolism in neoformed gall organs differs from that in uninfected roots. Depletion of (h)GSH content impaired nematode egg mass formation and modified the sex ratio. In addition, gene expression and metabolomic analyses showed a substantial modification of starch and γ-aminobutyrate metabolism and of malate and glucose content in (h)GSH-depleted galls. Interestingly, these modifications did not occur in (h)GSH-depleted roots. These various results suggest that (h)GSH have a key role in the regulation of giant cell metabolism. The discovery of these specific plant regulatory elements could lead to the development of new pest management strategies against nematodes.

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“…Initially, two chloroplastic thioredoxins, the f and m type, were reported as the light-dependent post-translational regulators of metabolic activity. At present, several other types of thioredoxins have been reported, which are classified according to their structure, target proteins, and localization (Chibani et al, 2010). The high multitude of thioredoxin-like proteins in photosynthetic organisms is surprising and challenging in terms of the identification of their specific functions by reverse genetic approaches.…”

Section: Thiol-based Redox Regulators Of Higher Plantsmentioning

confidence: 99%

Thiol-based redox control of enzymes involved in the tetrapyrrole biosynthesis pathway in plants

Richter¹,

Grimm²

2013

Front. Plant Sci.

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The last decades of research brought substantial insights into tetrapyrrole biosynthetic pathway in photosynthetic organisms. Almost all genes have been identified and roles of seemingly all essential proteins, leading to the synthesis of heme, siroheme, phytochromobilin, and chlorophyll (Chl), have been characterized. Detailed studies revealed the existence of a complex network of transcriptional and post-translational control mechanisms for maintaining a well-adjusted tetrapyrrole biosynthesis during plant development and adequate responses to environmental changes. Among others one of the known post-translational modifications is regulation of enzyme activities by redox modulators. Thioredoxins and NADPH-dependent thioredoxin reductase C (NTRC) adjust the activity of tetrapyrrole synthesis to the redox status of plastids. Excessive excitation energy of Chls in both photosystems and accumulation of light-absorbing unbound tetrapyrrole intermediates generate reactive oxygen species, which interfere with the plastid redox poise. Recent reports highlight ferredoxin-thioredoxin and NTRC-dependent control of key steps in tetrapyrrole biosynthesis in plants. In this review we introduce the regulatory impact of these reductants on the stability and activity of enzymes involved in 5-aminolevulinic acid synthesis as well as in the Mg-branch of the tetrapyrrole biosynthetic pathway and we propose molecular mechanisms behind this redox control.

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The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment

Cited by 30 publications

References 164 publications

The Redox-Sensitive Chloroplast Trehalose-6-Phosphate Phosphatase AtTPPD Regulates Salt Stress Tolerance

The Redox-Sensitive Chloroplast Trehalose-6-Phosphate Phosphatase AtTPPD Regulates Salt Stress Tolerance

(Homo)glutathione Deficiency Impairs Root-knot Nematode Development in Medicago truncatula

Thiol-based redox control of enzymes involved in the tetrapyrrole biosynthesis pathway in plants

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