Plant glutaredoxins: still mysterious reducing systems

@article{Rouhier2004PlantGS,
  title={Plant glutaredoxins: still mysterious reducing systems},
  author={Nicholas Rouhier and Eric Gelhaye and Jean-Pierre Jacquot},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2004},
  volume={61},
  pages={1266-1277}
}
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… Expand

Figures, Tables, and Topics from this paper

Thioredoxins inArabidopsis and other plants
TLDR
The numerous thioredoxin types encoded by the Arabidopsis genome are described, and evidence that they are present in all higher plants is provided, and some results suggest cross-talk between thiOREDoxins and glutaredoxins, the second family of disulfide dithiol reductase. Expand
Monothiol glutaredoxins: a common domain for multiple functions
TLDR
Monothiol glutaredoxins share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators. Expand
Identification of plant glutaredoxin targets.
TLDR
The determination of Grx target proteins using a mutated poplar Grx, various tissular and subcellular plant extracts, and liquid chromatography coupled to tandem mass spectrometry detection suggest that the interaction could occur randomly either with exposed cysteinyl disulfide bonds formed within or between target proteins or with mixed disulfides between a protein thiol and glutathione. Expand
Glutaredoxins and thioredoxins in plants.
TLDR
The view of plant thioredoxins and glutaredoxins was profoundly modified by the sequencing programs which revealed an unexpected number of genes encoding not only the previously identified disulfide reductases, but also numerous new types. Expand
Chapter 11 Glutaredoxins in Development and Stress Responses of Plants
TLDR
Comparisons of the involved signaling pathways that have been thus far considered to be unrelated with one another reveal that similar protein molecules, CC-type GRXs as well as TGA transcription factors, seem to have been recruited to participate in these different pathways. Expand
Identification of novel targets of cyanobacterial glutaredoxin.
TLDR
The studies suggest Grx2061 in cyanobacteria plays an important role in redox network and its targets are as extensive as that in other organisms. Expand
Redox Modulation Matters: Emerging Functions for Glutaredoxins in Plant Development and Stress Responses
TLDR
Emphasis is placed on the recently emerging functions for GRXs in floral organ development and disease resistance and the current knowledge of plant GRZs in the assembly and delivery of iron-sulfur clusters, oxidative stress responses and arsenic resistance. Expand
Thioredoxins and glutaredoxins: unifying elements in redox biology.
TLDR
The ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation and add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. Expand
Substrate specificity of thioredoxins and glutaredoxins – towards a functional classification
TLDR
These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases, and instead demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies. Expand
Engineered mutated glutaredoxins mimicking peculiar plant class III glutaredoxins bind iron-sulfur centers and possess reductase activity.
TLDR
The functionally important, hydrophobic GALWL C-terminal end, found in most class III glutaredoxins, prevents expression in Escherichia coli, and changing the C-Terminal end of GrxS7.2, a genuine classIII glutaredoxin, allowed purifying some holoproteins. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 86 REFERENCES
Characterization of the redox properties of poplar glutaredoxin.
TLDR
The poplar glutaredoxin can serve as an electron donor to the bacterial 3'-phosphoadenylylsulfate reductase as it supports both the catalysis by the enzyme in vitro and complements a methionine auxotroph strain of Escherichia coli. Expand
Grx5 Glutaredoxin Plays a Central Role in Protection against Protein Oxidative Damage inSaccharomyces cerevisiae
TLDR
The synthetic lethality of the grx5 and grx2 mutations on one hand and ofgrx5 with thegrx3 grx4 combination on the other points to a complex functional relationship among yeast glutaredoxins, with Grx5 playing a specially important role in protection against oxidative stress both during ordinary growth conditions and after externally induced damage. Expand
PLANT THIOREDOXIN SYSTEMS REVISITED.
TLDR
Recent developments that have provided new insights into the structures of several components and into the mechanism of action of the thioredoxin systems in plants are summarized. Expand
A strategy for the identification of proteins targeted by thioredoxin
TLDR
These findings open the door to the identification of proteins targeted by thioredoxin in a wide range of systems, thereby enhancing the understanding of its function and extending its technological and medical applications. Expand
Proteomics gives insight into the regulatory function of chloroplast thioredoxins
Thioredoxins are small multifunctional redox active proteins widely if not universally distributed among living organisms. In chloroplasts, two types of thioredoxins (f and m) coexist and playExpand
Biochemical Characterization of Yeast Mitochondrial Grx5 Monothiol Glutaredoxin*
TLDR
The disulfide bond in Grx5 could be reduced by GSH but at a rate at least 20 times slower than that observed for the reduction of glutaredoxin 1 from E. coli, which could suggest that GSH may not be the physiologic reducing agent of GrX5. Expand
Identification and characterization of a mitochondrial thioredoxin system in plants
TLDR
The thiOREDoxin and the NADPH-dependent thioredoxin reductase described here are proposed to constitute a functional plant mitochondrial thioringoxin system. Expand
Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase.
TLDR
The C domain can substitute for glutaredoxin in vivo as demonstrated by complementation of an E. coli mutant, underscoring the functional similarity between the two enzymes. Expand
Glutaredoxin-dependent Peroxiredoxin from Poplar
TLDR
To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed and it is shown that Grx can act in this reaction either via a dithiol or a monothiol pathway. Expand
Reactivity of Glutaredoxins 1, 2, and 3 fromEscherichia coli Shows That Glutaredoxin 2 Is the Primary Hydrogen Donor to ArsC-catalyzed Arsenate Reduction*
TLDR
Glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC, suggesting that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase. Expand
...
1
2
3
4
5
...