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Registros recuperados: 17
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An atypical catalytic mechanism involving three cysteines of thioredoxin Inra
Koh, C.S.; Navrot, N.; Didierjean, C.; Rouhier, N.; Hirasawa, M.; Knaff, D.B.; Wingsle, G.; Samian, R.; Jacquot, J.P.; Corbier, C.; Gelhaye, E..
Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys4) and two (Cys58 and Cys61) in the classical thioredoxin active site (57WCGPC61). The property of a mutant in which Cys58 was replaced by serine demonstrates that it is responsible for the initial nucleophilic attack during the catalytic cycle. The observation that the C4S mutant is inactive in the presence of Grx but fully active when dithiothreitol is used as a reductant indicates that Cys4 is required for the regeneration of PtTrxh4 by Grx. Biochemical and x-ray crystallographic studies...
Tipo: Journal Article Palavras-chave: THIOREDOXINE H; CATALYSE; CYSTEINE; OXYDOREDUCTION; NADPH:THIOREDOXINE REDUCTASE; PONT DISULFITE.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008b12c63ec&uri=/notices/prodinra1/2010/11/
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Cadmium induced mitochondrial redox changes in germinating pea seed Inra
Smiri, M.; Chaoui, A.; Rouhier, N.; Chibani, K.; Gelhaye, É.; Jacquot, J.P.; El Ferjani, E.
Mitochondria play an essential role in producing the energy required for seedling growth following imbibition. Heavy metals, such as cadmium impair mitochondrial functioning in part by altering redox regulation. The activities of two protein redox systems present in mitochondria, thioredoxin (Trx) and glutaredoxin (Grx), were analysed in the cotyledons and embryo of pea (Pisum sativum L.) germinating seeds exposed to toxic Cd concentration. Compared to controls, Cd-treated germinating seeds showed a decrease in total soluble protein content, but an increase in –SH content. Under Cd stress conditions, Grx and glutathione reductase (GR) activities as well as glutathione (GSH) concentrations decreased both in cotyledons and the embryo. Similar results were...
Tipo: Journal Article Palavras-chave: PEA; COTYLEDONS; EMBRYO; HEAVY METALS; CADMIUM; GERMINATING SEEDS; MITOCHONDRIA; REDOX; THIOREDOXIN; GLUTAREDOXIN; GLUTATHIONE REDUCTASE; NADPH-DEPENDENT THIOREDOXIN REDUCTASE; NAD(P)H OXIDASE; OXIDATIVE STRESS.
Ano: 2010 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201014da3708&uri=/notices/prodinra1/2010/11/
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Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe–2S] clusters Inra
Bandyopadhyay, S; Gama, F.; Molina-Navarro, MM; Gualberto, JM; Claxton, R; Naik, SG; Huynh, BH; Herrero, E; Jacquot, J.P.; Johnson, MK; Rouhier, N..
Glutaredoxins (Grxs) are small oxidoreductases that reduce disulphide bonds or protein-glutathione mixed disulphides. More than 30 distinct grx genes are expressed in higher plants, but little is currently known concerning their functional diversity. This study presents biochemical and spectroscopic evidence for incorporation of a [2Fe–2S] cluster in two heterologously expressed chloroplastic Grxs, GrxS14 and GrxS16, and in vitro cysteine desulphurase-mediated assembly of an identical [2Fe–2S] cluster in apo-GrxS14. These Grxs possess the same monothiol CGFS active site as yeast Grx5 and both were able to complement a yeast grx5 mutant defective in Fe–S cluster assembly. In vitro kinetic studies monitored by CD spectroscopy indicate that [2Fe–2S] clusters...
Tipo: Journal Article Palavras-chave: CHLOROPLAST; GLUTAREDOXIN; IRON–SULPHUR PROTEIN; PLANT.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010131c0563&uri=/notices/prodinra1/2010/07/
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Effects of propiconazole on extra-cellular enzymes involved in nutrient mobilization during Trametes versicolor wood colonization Inra
Lekounougou, S.; Jacquot, J.P.; Gérardin, P.; Gelhaye, É..
The effects of propiconazole on extra-cellular enzyme levels in Trametes versicolor have been investigated during wood colonization and degradation. The working hypothesis was that the biocide could alter metabolic pathways, which could lead to an alteration of extra-cellular enzyme production. In the presence of a propiconazole sub-lethal concentration, the wood degradation rate decrease concomitantly with the lag phase of fungal development observed during wood colonisation. The pattern of production of enzymes involved in polysaccharide degradation (b-glucosidases, glucuronidases, cellobiohydrolases), nitrogen (leucine aminopeptidase) and phosphorus (acid phosphatase) mobilization was only slightly altered in the presence of the biocide. In experiments...
Tipo: Journal Article Palavras-chave: PROPICONAZOLE; TRIAZOLE; CHAMPIGNON LIGNIVORE; TRAITEMENT CHIMIQUE; MECANISME ACTION; ENZYME EXTRA-CELLULAIRE; B-GLUCOSIDASE; GLUCURONIDASE; B-CELLOBIOSIDASE; LEUCINE AMINOPEPTIDASE; PHOSPHATASE ACIDE; CHITINASE; CAFEINE; CROISSANCE FONGIQUE; INHIBITION; PRESERVATION DU BOIS ACID PHOSPHATASE; BETA-GLUCOSIDASE; BIOCIDES; CAFFEINE; CHITINASE; COLONIZATION; ENZYME ACTIVITY; ENZYMES; MICROBIAL DEGRADATION; MOBILIZATION; NUTRIENTS; PROPICONAZOLE; WOOD PRESERVATION.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010d5b49ffa&uri=/notices/prodinra1/2010/11/
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Evolution and diversity of glutaredoxins in photosynthetic organisms Inra
Couturier, J.; Jacquot, J.P.; Rouhier, N..
The genome sequencing of prokaryotic and eukaryotic photosynthetic organisms enables a comparative genomic study of the glutaredoxin (Grx) family. The analysis of 58 genomes, using a specific motif composed of the active site sequence and of amino acids involved in glutathione binding, led to an updated classification of Grxs into six classes. Only two classes (I and II) are common to all photosynthetic organisms. Eukaryotes and cyanobacteria have two specific Grx classes (classes III and IV and classes V and VI, respectively). The classes IV, V and VI have not yet been identified and contain multimodular Grx fusions. In addition, putative Grx partners were identified from the presence of fusion proteins, the conservation of gene order in bacterial...
Tipo: Journal Article Palavras-chave: MONOTHIOL GLUTAREDOXINS; THIOREDOXIN REDUCTASE; BIOCHEMICAL-CHARACTERIZATION; TGA FACTORS; GLUTATHIONE; PEROXIREDOXIN; PROTEINS; SYSTEMS; CLUSTER; DOMAIN; EVOLUTION; GENOMIC; GLUTAREDOXIN; PHOTOSYNTHETIC ORGANISMS .
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20108448f35f&uri=/notices/prodinra1/2010/10/
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Functional analysis and expression characteristics of chloroplastic Prx IIE Inra
Gama, F.; Bréhélin, C; Gelhaye, É.; Meyer, Y; Jacquot, J.P.; Rey, P; Rouhier, N..
Peroxiredoxins (Prxs) are ubiquitous thiol-dependent peroxidases capable of eliminating a variety of peroxides through reactive catalytic cysteines, which are regenerated by reducing systems. Based on amino acid sequences and their mode of catalysis, five groups of thiol peroxidases have been distinguished in plants, and type II Prx is one of them with representatives in many sub-cellular compartments. The mature form of poplar chloroplastic Prx IIE was expressed as a recombinant protein in Escherichia coli. The protein is able to reduce H2O2 and tert-butyl hydroperoxide and is regenerated by both glutaredoxin (Grx) and thioredoxin (Trx) systems. Nevertheless, compared with Trxs, Grxs, and more especially chloroplastic Grx S12, are far more efficient...
Tipo: Journal Article Palavras-chave: CHLOROPLAST GENETICS; FUNCTIONAL GENOMICS; GENE EXPRESSION; GENES; ARABIDOPSIS THALIANA; PLANTS.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010720c64a1&uri=/notices/prodinra1/2011/02/
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Functional and structural aspects of poplar cytosolic and plastidial type A methionine sulfoxide reductases Inra
Rouhier, N.; Kauffmann, B.; Tete-Favier, F.; Palladino, P.; Gans, P.; Branlant, G.; Jacquot, J.P.; Boschi-Muller, S..
The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys46 is the catalytic cysteine, and the two C-terminal cysteines, Cys196 and Cys202, are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure,...
Tipo: Journal Article Palavras-chave: METHIONINE SULFOXYDE REDUCTASE; ENZYME; FONCTION; STRUCTURE; GENE; ENZYME RECOMBINANT; REDUCTION; CYSTEINE; ANALYSE BIOCHIMIQUE; ANALYSE ENZYMATIQUE; CATALYSE; RAYON X POPULUS TRICHOCARPA.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20104994a2c3&uri=/notices/prodinra1/2010/11/
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Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer Inra
Noguera-Mazon, V.; Lemoine, J.; Walker, O.; Rouhier, N.; Salvador, A.; Jacquot, J.P.; Lancelin, J.M.; Krimm, I..
1-Cys peroxiredoxins (1-Cys Prxs) are antioxidant enzymes that catalyze the reduction of hydroperoxides into alcohols using a strictly conserved cysteine. 1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) {pi} via the formation of a GST-Prx heterodimer and Prx glutathionylation. In contrast, 1-Cys D-Prxs, homologous to human PrxV, are reactivated by the glutaredoxin-glutathione system through an unknown mechanism. To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR. This work reveals that the Prx can be glutathionylated on its active site cysteine. Evidences are reported that the...
Tipo: Journal Article Palavras-chave: PEROXIREDOXINE; HYDROPEROXYDE; CYSTEINE; RMN; RESONANCE MAGNETIQUE NUCLEAIRE PEROXIREDOXIN; HYDROPEROXIDE; CYSTEINE; NMR; SPECTROMETRY.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20074bcd41f3&uri=/notices/prodinra1/2010/11/
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Immunolocalization of non-symbiotic hemoglobins during somatic embryogenesis in chicory Inra
Smagghe, B.; Blervacq, A.S.; Blassiau, C.; Decottignies, J.P.; Jacquot, J.P.; Hargrove, M.S.; Hilbert, J.L..
Hemoglobins are ancient O2‑binding proteins, ubiquitously found in eukaryotes. They have been categorized as symbiotic, nonsymbiotic and truncated hemoglobins. We have investigated the cellular localization of nonsymbiotic hemoglobin proteins during somatic embryogenesis in Cichorium hybrid leaves (Cichorium intybus L. var. sativum x C. endivia var. latifolia) using immunolocalization technique. These proteins were detected during the two steps of culture: induction and expression. In leaves, hemoglobins colocalised with plastids, which were dispersed in the parietal cytoplasm as well as in the two guard cells of a stomata, but not in epidermis cells. Upon induction of embryogenesis, in the dark, this pattern disappeared. During the induction phase, where...
Tipo: Journal Article Palavras-chave: CHICORY; IMMUNOLOCALIZATION; NON SYMBIOTIC HEMOGLOBIN; SOMATIC EMBRYOGENESIS; CICHORIUM INTYBUS L. VAR. SATIVUM X C. ENDIVIA VAR. LATIFOLIA.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20107f17f74b&uri=/notices/prodinra1/2010/07/
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Introduction Inra
Jacquot, J.P.; Rouhier, N..
Photosynthesis occurs in vastly different forms, for e.g. some prokaryotes perform anoxygenic photosynthesis, and on the other hand, cyanobacteria, algae and land plants use oxygenic photosynthesis. Likewise, in land plants, most organisms rely on so-called C3 photosynthesis, but several tropical species as maize or sugarcane use a variant called C4 photosynthesis in which the first photosynthetic product is malate, a 4 carbon compound, rather than phosphoglyceric acid the more classical 3 carbon compound. Another example of the variation of the photosynthetic mode is found in so-called CAM (crassulacean acid metabolism) plants where CO2 fixation takes place at night rather than during the light, enabling these plants to resist extreme climatic conditions.
Tipo: Journal Article Palavras-chave:  .
Ano: 2010 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010143287e5&uri=/notices/prodinra1/2010/10/
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Letter to the Editor: 1H, 13C and 15N NMR assignment of the homodimeric poplar phloem type II peroxiredoxin Inra
Bouillac, S.; Rouhier, N.; Tsan, P.; Jacquot, J.P.; Lancelin, J.M..
Tipo: Journal Article Palavras-chave: DEUTERATION; GLUTAREDOXINE; HYDROPEROXIDE; RMN; RESONANCE MAGNETIQUE NUCLEAIRE; PEROXIREDOXINE; PLANTE DEUTERATION; GLUTAREDOXIN; HYDROPEROXIDE; NMR; PEROXIREDOXIN; PLANT.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007238dad88&uri=/notices/prodinra1/2010/11/
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Letter to the Editor: 1H, 13C and 15N resonance assignment of the reduced form of thioredoxin h1 from Poplar, a CPPC active site variant Inra
Coudevylle, N.; Thureau, A.; Hemmerlin, C.; Gelhaye, E.; Jacquot, J.P.; Cung, M.T..
Tipo: Journal Article Palavras-chave: DISULPHIDE OXYDOREDUCTASE; RESONANCE; THIOREDOXINE DISULFIDE OXIDOREDUCTASE; RESONANCE ASSIGNMENT; THIOREDOXIN.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200798452ac6&uri=/notices/prodinra1/2010/11/
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Letter to the Editor: 1H, 13C and 15N resonance assignments of poplar phloem glutaredoxin Inra
Noguera, V.; Rouhier, N.; Krimm, I.; Jacquot, J.P.; Lancelin, J.M..
Tipo: Journal Article Palavras-chave: DISULPHIDE OXIDOREDUCTASE; GLUTAREDOXINE; PEROXIREDOXINE DISULFIDE OXIDOREDUCTASE; GLUTAREDOXIN; PEROXIREDOXIN; POPLAR.
Ano: 2004 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20077b374d1d&uri=/notices/prodinra1/2010/11/
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Letter to the Editor: 1H, 15N, and 13C resonance assignments of reduced glutaredoxin C1 from Populus tremula x tremuloides Inra
Feng, Y.; Rouhier, N.; Jacquot, J.P.; Xia, B..
Tipo: Journal Article Palavras-chave: GLUTAREDOXINE; RMN; RESONANCE MAGNETIQUE NUCLEAIRE GLUTAREDOXIN; NMR ASSIGNMENTS; POPLAR.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20076779d9d0&uri=/notices/prodinra1/2010/11/
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Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site Inra
Couturier, J.; Koh, C.S.; Zaffagnini, M.; Winger, A.M.; Gualberto, J.M.; Corbier, C.; Decottignies, P.; Jacquot, J.P.; Lemaire, S.D.; Didierjean, C.; Rouhier, N..
Glutaredoxins (Grxs) are efficient catalysts for the reduction of mixed disulfides in glutathionylated proteins, using glutathione or thioredoxin reductases for their regeneration. Using GFP fusion, we have shown that poplar GrxS12, which possesses a monothiol 28WCSYS32 active site, is localized in chloroplasts. In the presence of reduced glutathione, the recombinant protein is able to reduce in vitro substrates, such as hydroxyethyldisulfide and dehydroascorbate, and to regenerate the glutathionylated glyceraldehyde-3-phosphate dehydrogenase. Although the protein possesses two conserved cysteines, it is functioning through a monothiol mechanism, the conserved C terminus cysteine (Cys87) being dispensable, since the C87S variant is fully active in all...
Tipo: Journal Article Palavras-chave: ESCHERICHIA-COLI GLUTAREDOXIN; GRX5 MONOTHIOL GLUTAREDOXIN; NMR SOLUTION STRUCTURE; IRON-SULFUR CLUSTER; MIXED DISULFIDE; DIRECTED MUTAGENESIS; BIOCHEMICAL-CHARACTERIZATION; CHLAMYDOMONAS-REINHARDTII; PHOTOSYNTHETIC ORGANISMS; SACCHAROMYCES-CEREVISIAE.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20104988b76a&uri=/notices/prodinra1/2010/10/
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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 Inra
Chibani, K.; Couturier, J.; Selles, B.; Jacquot, J.P.; Rouhier, N..
The post-translational modification consisting in the formation/reduction of disulfide bonds has been the subject of intense research in plants since the discovery in the 1970s that many chloroplastic enzymes are regulated by light through dithiol–disulfide exchange reactions catalyzed by oxidoreductases called thioredoxins (Trxs). Further biochemical and proteomic studies have considerably increased the number of target enzymes and processes regulated by these mechanisms in many sub-cellular compartments. Recently, glutathionylation, a modification consisting in the reversible formation of a glutathione adduct on cysteine residues, was proposed as an alternative redox regulation mechanism. Glutaredoxins (Grxs), proteins related to Trxs, are efficient...
Tipo: Journal Article Palavras-chave: NADP-MALATE DEHYDROGENASE; METHIONINE SULFOXIDE REDUCTASE; FERREDOXIN-THIOREDOXIN REDUCTASE; GENOME-WIDE ANALYSIS; IRON-SULFUR PROTEIN; ARABIDOPSIS-THALIANA; CHLAMYDOMONAS-REINHARDTII; OXIDATIVE STRESS; GLUTATHIONE-PEROXIDASE; PHOTOOXIDATIVE STRESS; CHLOROPLAST; GLUTAREDOXIN; PHOTOSYNTHESIS; STRESS; THIOREDOXIN.
Ano: 2010 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010751aa923&uri=/notices/prodinra1/2010/10/
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The fungal glutathione S-transferase system. Evidence of new classes in the wood-degrading basidiomycete Phanerochaete chrysosporium Inra
Morel, M.; Ngadin, A.A.; Droux, M.; Jacquot, J.P.; Gelhaye, É..
The recent release of several basidiomycete genome sequences allows an improvement of the classification of fungal glutathione S-transferases (GSTs). GSTs are well-known detoxification enzymes which can catalyze the conjugation of glutathione to non-polar compounds that contain an electrophilic carbon, nitrogen, or sulfur atom. Following this mechanism, they are able to metabolize drugs, pesticides, and many other xenobiotics and peroxides. A genomic and phylogenetic analysis of GST classes in various sequenced fungi—zygomycetes, ascomycetes, and basidiomycetes—revealed some particularities in GST distribution, in comparison with previous analyses with ascomycetes only. By focusing essentially on the wooddegrading basidiomycete Phanerochaete chrysosporium,...
Tipo: Journal Article Palavras-chave: BETA-ARYL ETHER; POLYCYCLIC AROMATIC-HYDROCARBONS; PRION PROTEIN URE2; SACCHAROMYCES-CEREVISIAE; OMEGA-CLASS; OXIDATIVE STRESS; SCHIZOSACCHAROMYCES-POMBE; PSEUDOMONAS-PAUCIMOBILIS; METABOLIZING ENZYMES; MOLECULAR-CLONING; PHANEROCHAETE CHRYSOSPORIUM; GLUTATHIONE S-TRANSFERASE; ETHERASE; OMEGA CLASS GST; URE2P; GTT.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20107588cb2a&uri=/notices/prodinra1/2010/10/
Registros recuperados: 17
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