Redox Signal Transduction in Plant Metabolism

Mora-Garcı́a, Santiago; Stolowicz, Fabiana G.; Wolosiuk, Ricardo A.

doi:10.1002/9780470988640.ch6

Cited by 4 publications

(3 citation statements)

References 201 publications

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“…By contrast to the extensive literature on the redox modulation of different enzyme activities in chloroplasts and non‐photosynthetic systems, mainly via thiol–disulfide exchange [13–16], systematic efforts to examine the opposite action of non‐redox processes on redox reactions are scarce. Most biochemical research on 2‐Cys Prx has studied the interplay between the stimuli and the abundance of reductants and oxidants (thermodynamic control), whereas the catalytic features (kinetic control) have been less clear.…”

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ATP‐dependent modulation and autophosphorylation of rapeseed 2‐Cys peroxiredoxin

et al. 2008

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2-Cys peroxiredoxins (2-Cys Prx) are ubiquitous thiol-containing peroxidases that have been implicated in antioxidant defense and signal transduction. Although their biochemical features have been extensively studied, little is known about the mechanisms that link the redox activity and non-redox processes. Here we report that the concerted action of a nucleoside triphosphate and Mg(2+) on rapeseed 2-Cys Prx reversibly impairs the peroxidase activity and promotes the formation of high molecular mass species. Using protein intrinsic fluorescence in the analysis of site-directed mutants, we demonstrate that ATP quenches the emission intensity of Trp179, a residue close to the conserved Cys175. More importantly, we found that ATP facilitates the autophosphorylation of 2-Cys Prx when the protein is successively reduced with thiol-bearing compounds and oxidized with hydroperoxides or quinones. MS analyses reveal that 2-Cys Prx incorporates the phosphoryl group into the Cys175 residue yielding the sulfinic-phosphoryl [Prx-(Cys175)-SO(2)PO(3)(2-)] and the sulfonic-phosphoryl [Prx-(Cys175)-SO(3)PO(3)(2-)] anhydrides. Hence, the functional coupling between ATP and 2-Cys Prx gives novel insights into not only the removal of reactive oxygen species, but also mechanisms that link the energy status of the cell and the oxidation of cysteine residues.

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ATP‐dependent modulation and autophosphorylation of rapeseed 2‐Cys peroxiredoxin

et al. 2008

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“…Moreover, the thioredoxin family of proteins continues to grow, with at least 19 isoforms in the Arabidopsis genome from the f‐, h‐, m‐, o‐, x‐ and y‐types. To further complicate the picture, there are many other thioredoxin‐fold containing proteins, including some 31 glutaredoxins and several other thioredoxin‐related proteins in Arabidopsis, although the extent to which these proteins play a regulatory role in metabolism remains to be established (Mora‐Garcia et al ., 2006).…”

Section: Redox Signallingmentioning

confidence: 99%

Signalling in primary metabolism

Finkemeier

2006

New Phytologist

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“…Therefore, the following experiments were designed to investigate more thoroughly this issue with the counterpart of higher plant chloroplasts. In this scenario, chloroplast fructose-1,6-bisphosphatase (CFBPase) is an exemplary enzyme of photosynthetic CO 2 assimilation whose catalytic capacity is markedly stimulated by light via the ferredoxin-thioredoxin system [8][9][10][11]. Site-directed mutagenesis revealed that the constituent polypeptide (ca.…”

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confidence: 99%