Characterization of the Redox Properties of Poplar Glutaredoxin

Rouhier, Nicolas; Vlamis-Gardikas, Alexios; Lillig, Christopher Horst; Berndt, Carsten; Schwenn, Jens D.; Holmgren, Arne; Jacquot, Jean‐Pierre

doi:10.1089/152308603321223504

Cited by 35 publications

(24 citation statements)

References 44 publications

(46 reference statements)

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“…Finally, the cell specific distribution of thioredoxins could have played a role in the outcome of the experiment. It is known that PaAPR and EcPAPR are able to use thioredoxins from diverse sources including those from plants (Wagner et al 1978;Schwenn and Schriek 1987;Bick et al 2000;Rouhier et al 2003), although how well they can utilize specific Z. mays thioredoxins is unknown. Furthermore, the cell specific distribution of thioredoxins and the capacity to reduce thioredoxins is not well characterized in Z. mays (Matsumura et al 1999).…”

Section: Discussion Of the Transgenic Z Mays Experimentsmentioning

confidence: 99%

The role of 5′-adenylylsulfate reductase in controlling sulfate reduction in plants

et al. 2005

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Cysteine is the first organic product of sulfate assimilation and as such is the precursor of all molecules containing reduced sulfur including methionine, glutathione, and their many metabolites. In plants, 5'-adenylylsulfate (APS) reductase is hypothesized to be a key regulatory point in sulfate assimilation and reduction. APS reductase catalyzes the two-electron reduction of APS to sulfite using glutathione as an electron donor. This paper reviews the experimental basis for this hypothesis. In addition, the results of an experiment designed to test the hypothesis by bypassing the endogenous APS reductase and its regulatory mechanisms are described. Two different bacterial assimilatory reductases were expressed in transgenic Zea mays, the thioredoxin-dependent APS reductase from Pseudomonas aeruginosa and the thioredoxin-dependent 3'-phosphoadenylylsulfate reductase from Escherichia coli. Each of them was placed under transcriptional control of the ubiquitin promoter and the protein products were targeted to chloroplasts. The leaves of transgenic Z. mays lines showed significant accumulation of reduced organic thiol compounds including cysteine, gamma-glutamylcysteine, and glutathione; and reduced inorganic forms of sulfur including sulfite and thiosulfate. Both bacterial enzymes appeared to be equally capable of deregulating the assimilative sulfate reduction pathway. The reduced sulfur compounds accumulated to such high levels that the transgenic plants showed evidence of toxicity. The results provide additional evidence that APS reductase is a major control point for sulfate reduction in Z. mays.

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Section: Discussion Of the Transgenic Z Mays Experimentsmentioning

confidence: 99%

The role of 5′-adenylylsulfate reductase in controlling sulfate reduction in plants

et al. 2005

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“…This is quite surprising since O. sativa possesses at least one type II Prx isoform (EST accession number BP184892). The poplar Grx characterized, which belongs to the same group of Grx, does not possess such an activity toward hydroperoxides [27]. Other known targets of Grx in A. thaliana are H + /Ca 2+ transporters called CAX1 and CAX4 for cation exchanger [21].…”

Section: The Functions Of Grx In Plants and In Other Organisms: Knownmentioning

confidence: 99%

Plant glutaredoxins: still mysterious reducing systems

Rouhier

Gelhaye

Jacquot

2004

CMLS, Cell. Mol. Life Sci.

192

169

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Glutaredoxins are ubiquitous oxidoreductases which are similar to thioredoxins and possess a typical glutathione-reducible CxxC or CxxS active site. We present here the current knowledge about these proteins in plants. At least 31 glutaredoxin genes are present in Arabidopsis thaliana, a value close to the thioredoxin gene number. Based essentially on active site sequences, a classification of these multiple genes is proposed. The specificity of the various apparently redundant forms within the glutaredoxin group or between glutaredoxin and thioredoxin can be analysed in terms of differential spatiotemporal expression of the genes, specificity vs. target proteins and mode of catalysis (glutathiolation/ deglutathiolation processes appear to be a specific function of glutaredoxin). Additional putative functions are proposed for plant glutaredoxins based on their targets in other organisms and in the light of the existence of hybrid proteins containing glutaredoxin modules in their N- or C-terminal part.

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“…We have recently undertaken an NMR study of the Populus tremula Prx-GSH-Grx system, in which the P. tremula Grx C4 targets a specific D (type II) Prx. [14][15][16] We have shown using NMR and crystal structure that P. tremula D-Prx is a non-covalent homodimer in solution, with a Prx-Prx interface similar to hyPrx5. 17,18 We present here an NMR study of the P. tremula Grx C4 in reducing medium.…”

Section: Introductionmentioning

confidence: 99%