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المؤلفون: Laura Carmen Terrón-Camero, Eliana Molina-Moya, Luisa M. Sandalio, María C. Romero-Puertas, M. Ángeles Peláez-Vico
المساهمون: Ministerio de Ciencia, Innovación y Universidades (España), European Commission, Ministerio de Educación, Cultura y Deporte (España), Ministerio de Economía, Industria y Competitividad (España)
المصدر: Journal of Experimental Botany
مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Redox signalling, Physiology, Plant Science, Biology, 01 natural sciences, Redox, Transcriptome, 03 medical and health sciences, chemistry.chemical_compound, Biotic stress, Gene Expression Regulation, Plant, Stress, Physiological, Gene, Review Papers, Fungal pathogens, Reactive nitrogen species, Genetics, Abiotic component, AcademicSubjects/SCI01210, Abiotic stress, fungi, food and beverages, Nitric oxide, Plants, Crosstalk (biology), 030104 developmental biology, chemistry, Reactive oxygen species, Oxidation-Reduction, Cadmium, 010606 plant biology & botany
الوصف: Reactive oxygen and nitrogen species and redox signals are at the crossroads of plant responses to abiotic and biotic stress and mediate plant-induced resistance/sensitivity, which mainly depends on the specific interaction.
Complex signalling pathways are involved in plant protection against single and combined stresses. Plants are able to coordinate genome-wide transcriptional reprogramming and display a unique programme of transcriptional responses to a combination of stresses that differs from the response to single stresses. However, a significant overlap between pathways and some defence genes in the form of shared and general stress-responsive genes appears to be commonly involved in responses to multiple biotic and abiotic stresses. Reactive oxygen and nitrogen species, as well as redox signals, are key molecules involved at the crossroads of the perception of different stress factors and the regulation of both specific and general plant responses to biotic and abiotic stresses. In this review, we focus on crosstalk between plant responses to biotic and abiotic stresses, in addition to possible plant protection against pathogens caused by previous abiotic stress. Bioinformatic analyses of transcriptome data from cadmium- and fungal pathogen-treated plants focusing on redox gene ontology categories were carried out to gain a better understanding of common plant responses to abiotic and biotic stresses. The role of reactive oxygen and nitrogen species in the complex network involved in plant responses to changes in their environment is also discussed.الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::655ee6fe10d667b7bad1c9f37407bd28Test
https://doi.org/10.1093/jxb/erab271Test -
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المؤلفون: Gokhan Cucun, Nil Demircan, Baris Uzilday
المساهمون: Ege Üniversitesi
المصدر: Plant Biotechnology Reports. 14:235-245
مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Alternative oxidase, Redox signalling, Arabidopsis thaliana, Mutant, Plant Science, medicine.disease_cause, 01 natural sciences, Plastid terminal oxidase, 03 medical and health sciences, medicine, chemistry.chemical_classification, Reactive oxygen species, biology, fungi, Wild type, food and beverages, Arsenic stress, biology.organism_classification, Heavy metal, 030104 developmental biology, Biochemistry, chemistry, biology.protein, Oxidative stress, Alternative electron sinks, 010606 plant biology & botany, Biotechnology, Peroxidase
الوصف: The element arsenic (As) is a non-essential metalloid that is found naturally in all soils and at high concentrations it is toxic to plant cells. As (V) can act as a chemical analogue of phosphate, it can disrupt phosphate-related energy metabolism and lipid structure. in this study, the contribution of mitochondrial alternative oxidase (AOX) and chloroplastic plastid terminal oxidase (PTOX) to As (V) stress tolerance was investigated. Our data indicate that As (V) stress (100, 200 and 300 mu M) induces AOX gene expression by 3.3- to 10.5-fold depending on AOX gene, but not PTOX expression in wild-type A. thaliana plants. To further elucidate the role of AOX in As (V) stress tolerance, we utilized aox1a mutants and observed that aox1a mutants had decreased growth and higher oxidative stress damage under stress conditions, while there were no differences under control conditions. Moreover, acclimation of aox1a plants to new cellular redox environment was investigated by measuring the activities of reactive oxygen species (ROS)-scavenging enzymes. Induction of mitochondrial MnSOD activity at 300 mu M As (V) was higher in aox1a plants (70%), when compared to wild type (43%). However, total ascorbate peroxidase and dehydroascorbate reductase activities were lower in aox1a plants when compared to wild type, which might explain higher oxidative damage observed in this genotype. on the other hand, NADPH oxidase activity, which is involved in ROS signaling, was lower in aox1a plants under normal conditions but a higher induction was observed with As (V) stress. Overall, our data indicate that AOX1a is involved in adaptation to As (V)-induced oxidative stress.
Korean Acad Sci & Technol, Assoc Acad & Sco Sci Asiaالوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9967cc874ad2e56d1ef269bc766161a5Test
https://doi.org/10.1007/s11816-020-00595-9Test -
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المؤلفون: Cesar Petri, Agustina Bernal-Vicente, José Antonio Hernández, Daniel Cantabella, Pedro Diaz-Vivancos
المساهمون: Producció Vegetal, Postcollita, European Commission, Ministerio de Economía y Competitividad (España), Universidad Politécnica de Cartagena, CSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA)
المصدر: International Journal of Molecular Sciences
Volume 19
Issue 11
IRTA Pubpro. Open Digital Archive
Institut de Recerca i Tecnologia Agroalimentàries (IRTA)
Digital.CSIC. Repositorio Institucional del CSIC
instname
International Journal of Molecular Sciences, Vol 19, Iss 11, p 3519 (2018)مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, mandelonitrile, Salt Stress, 01 natural sciences, lcsh:Chemistry, Mandelonitrile, chemistry.chemical_compound, salt-stress, lcsh:QH301-705.5, Chlorophyll fluorescence, Spectroscopy, chlorophyll fluorescence, Jasmonic acid, Salicylic acid, Prunus domestica, General Medicine, Plants, Genetically Modified, NPR1, Computer Science Applications, Biochemistry, Shoot, Redox signalling, Acetonitriles, salicylic acid, Thioredoxin h, Article, Catalysis, Soluble nutrients, Inorganic Chemistry, 03 medical and health sciences, Biosynthesis, biochemistry, Physical and Theoretical Chemistry, Molecular Biology, J8-1 plum line, Salt-stress, Organic Chemistry, redox signalling, soluble nutrients, Biosynthetic Pathways, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, chemistry, Salts, 010606 plant biology & botany
الوصف: Salinity is considered as one of the most important abiotic challenges that affect crop productivity. Plant hormones, including salicylic acid (SA), are key factors in the defence signalling output triggered during plant responses against environmental stresses. We have previously reported in peach a new SA biosynthetic pathway from mandelonitrile (MD), the molecule at the hub of the cyanogenic glucoside turnover in Prunus sp. In this work, we have studied whether this new SA biosynthetic pathway is also present in plum and the possible role this pathway plays in plant plasticity under salinity, focusing on the transgenic plum line J8-1, which displays stress tolerance via an enhanced antioxidant capacity. The SA biosynthesis from MD in non-transgenic and J8-1 micropropagated plum shoots was studied by metabolomics. Then the response of J8-1 to salt stress in presence of MD or Phe (MD precursor) was assayed by measuring: chlorophyll content and fluorescence parameters, stress related hormones, levels of non-enzymatic antioxidants, the expression of two genes coding redox-related proteins, and the content of soluble nutrients. The results from in vitro assays suggest that the SA synthesis from the MD pathway demonstrated in peach is not clearly present in plum, at least under the tested conditions. Nevertheless, in J8-1 NaCl-stressed seedlings, an increase in SA was recorded as a result of the MD treatment, suggesting that MD could be involved in the SA biosynthesis under NaCl stress conditions in plum plants. We have also shown that the plum line J8-1 was tolerant to NaCl under greenhouse conditions, and this response was quite similar in MD-treated plants. Nevertheless, the MD treatment produced an increase in SA, jasmonic acid (JA) and reduced ascorbate (ASC) contents, as well as in the coefficient of non-photochemical quenching (qN) and the gene expression of Non-Expressor of Pathogenesis-Related 1 (NPR1) and thioredoxin H (TrxH) under salinity conditions. This response suggested a crosstalk between different signalling pathways (NPR1/Trx and SA/JA) leading to salinity tolerance in the transgenic plum line J8-1.
This work was supported by the Spanish Ministry of Economy and Competitiveness (Projects AGL2014-52563-R and INIA-RTA2013-00026-C03-00). PDV and CP thank CSIC and UPCT, respectively, as well as the Spanish Ministry of Economy and Competitiveness for their ‘Ramon and Cajal’ research contract, co-financed by FEDER funds. This work was supported by the Spanish Ministry of Economy and Competitiveness (Projects AGL2014-52563-R and INIA-RTA2013-00026-C03-00).وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::956d6598b2fe4de7b77b3964da7db679Test
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المؤلفون: Mirko Zaffagnini, Andrea Bottoni, Francesca Sparla, Luisa Iommarini, Giuseppe Falini, Matteo Calvaresi, Roberto Orrù, Simona Fermani, Paolo Trost
المساهمون: Zaffagnini, Mirko, Fermani, Simona, Calvaresi, Matteo, Orrù, Roberto, Iommarini, Luisa, Sparla, Francesca, Falini, Giuseppe, Bottoni, Andrea, Trost, Paolo
المصدر: Antioxidants & Redox Signaling. 24:502-517
مصطلحات موضوعية: Models, Molecular, 0106 biological sciences, 0301 basic medicine, Cytoplasm, Chloroplasts, Protein Conformation, Physiology, Stereochemistry, Clinical Biochemistry, Arabidopsis, Dehydrogenase, 01 natural sciences, Biochemistry, Sulfenic Acids, 03 medical and health sciences, chemistry.chemical_compound, Protein structure, Oxidoreductase, Catalytic Domain, Cysteine, CYSTEINE, REDOX SIGNALLING, GAPDH, H2O2, SULPHENIC ACID, Molecular Biology, Cysteine metabolism, Glyceraldehyde 3-phosphate dehydrogenase, General Environmental Science, chemistry.chemical_classification, Binding Sites, biology, Glyceraldehyde-3-Phosphate Dehydrogenases, Hydrogen Peroxide, Cell Biology, Kinetics, 030104 developmental biology, chemistry, Thiol, biology.protein, General Earth and Planetary Sciences, Sulfenic acid, Oxidation-Reduction, Protein Binding, 010606 plant biology & botany
الوصف: Cysteines and H2O2 are fundamental players in redox signaling. Cysteine thiol deprotonation favors the reaction with H2O2 that generates sulfenic acids with dual electrophilic/nucleophilic nature. The protein microenvironment surrounding the target cysteine is believed to control whether sulfenic acid can be reversibly regulated by disulfide formation or irreversibly oxidized to sulfinates/sulfonates. In this study, we present experimental oxidation kinetics and a quantum mechanical/molecular mechanical (QM/MM) investigation to elucidate the reaction of H2O2 with glycolytic and photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana (cytoplasmic AtGAPC1 and chloroplastic AtGAPA, respectively).Although AtGAPC1 and AtGAPA have almost identical 3D structure and similar acidity of their catalytic Cys149, AtGAPC1 is more sensitive to H2O2 and prone to irreversible oxidation than AtGAPA. As a result, sulfenic acid is more stable in AtGAPA.Based on crystallographic structures of AtGAPC1 and AtGAPA, the reaction potential energy surface for Cys149 oxidation by H2O2 was calculated by QM. In both enzymes, sulfenic acid formation was characterized by a lower energy barrier than sulfinate formation, and sulfonate formation was prevented by very high energy barriers. Activation energies for both oxidation steps were lower in AtGAPC1 than AtGAPA, supporting the higher propensity of AtGAPC1 toward irreversible oxidation.QM/MM calculations coupled to fingerprinting analyses revealed that two Arg of AtGAPA (substituted by Gly and Val in AtGAPC1), located at 8-15 Å distance from Cys149, are the major factors responsible for sulfenic acid stability, underpinning the importance of long-distance polar interactions in tuning sulfenic acid stability in native protein microenvironments.
وصف الملف: STAMPA
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee0be9dee563a683a40e4ae965971eb3Test
https://doi.org/10.1089/ars.2015.6417Test -
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المؤلفون: Harune Endo, Toshiki Uji, Hiroyuki Mizuta
المصدر: Frontiers in Plant Science
Frontiers in Plant Science, Vol 11 (2020)مصطلحات موضوعية: 0106 biological sciences, 0301 basic medicine, Pyropia, Ethylene, sexual reproduction, Plant Science, lcsh:Plant culture, plant hormone, medicine.disease_cause, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, medicine, ethylene, 1-Aminocyclopropane-1-carboxylic acid, lcsh:SB1-1110, Original Research, red algae, NADPH oxidase, Cycloleucine, biology, redox signalling, Glutathione, biology.organism_classification, Sexual reproduction, 030104 developmental biology, chemistry, Biochemistry, 1-aminocylopropane-1-carboxylic acid, biology.protein, Plant hormone, Oxidative stress, 010606 plant biology & botany
الوصف: The transition from the vegetative to sexually reproductive phase is the most dynamic change to occur during a plant's life cycle. In the present study, we showed that the ethylene precursor 1-aminocylopropane-1-carboxylic acid (ACC) induces sexual reproduction in the marine red alga Pyropia yezoensis independently from ethylene. Exogenous application of ACC, which contains a three membered carbocyclic ring, promoted the formation of spermatia and carporspores in gametophytes, whereas ethephon, an ethylene-releasing compound, did not stimulate sexual reproduction. In addition, an ACC analog, 1-aminocyclobutane-1-carboxylic acid (ACBC), which contains a four membered carbocyclic ring, promoted sexual reproduction and enhanced tolerance to oxidative stress in the same manner as ACC, but 1-aminocyclopentane-1-carboxylic acid (cycloleucine; which contains a cyclopentane ring) did not. The application of ACC increased the generation of reactive oxygen species (ROS) and induced the expression of PyRboh gene encoding NADPH oxidase. ACC also stimulated the synthesis of ascorbate (AsA) by inducing transcripts of PyGalLDH, which encodes galactono-1,4-lactone dehydrogenase, the catalyst for the final enzymatic step of the AsA biosynthetic pathway. Conversely, ACC caused a decrease in the synthesis of glutathione (GSH) by repressing transcripts of PyGCL, which encodes glutamate cysteine ligase, the catalyst for the rate-limiting step in the formation of GSH. These results suggest a possible role played by ACC as a signaling molecule independent from ethylene in the regulation of sexual reproduction through alterations to the redox state in P. yezoensis.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38f8a7fca5a751eadddfb0dd4dfffa28Test
http://hdl.handle.net/2115/77629Test -
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المؤلفون: Jean-Philippe Reichheld, Francisco Javier Cejudo, Nicolas Rouhier, José A. Traverso, Andreas J. Meyer
المساهمون: Universidad de Sevilla, Institut für Nutzpflanzenwissenschaften und Ressourcenschutz (INRES), Rheinische Friedrich-Wilhelms-Universität Bonn, Université de Perpignan Via Domitia (UPVD), Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Universidad de Granada (UGR), Instituto de Bioquímica Vegetal y Fotosíntesis (IBVF), Universidad de Sevilla-Centro de Investigaciones Científicas Isla de la Cartuja, INRES-Chemical Signalling, Laboratoire Génome et développement des plantes (LGDP), Université de Perpignan Via Domitia (UPVD)-Centre National de la Recherche Scientifique (CNRS), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Estacion Experimental del Zaidin (CSIC), Consejo Superior de Investigaciones Científicas [Spain] (CSIC), Instituto de Bioquimica Vegetal y Fotosintesis (IBVF), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Estación Experimental del Zaidín (EEZ)
المصدر: Frontiers in Plant Science, Vol 5 (2014)
Thiol-based redox homeostasis and signalling
Frontiers in Plant Science
Frontiers in Plant Science, Frontiers, 2014, 5, pp.1-3. ⟨10.3389/fpls.2014.00266⟩
Digibug. Repositorio Institucional de la Universidad de Granada
instname
Frontiers in Plant Science, Frontiers, 2014, 5, pp.450-450. ⟨10.3389/fpls.2014.00266⟩
Digital.CSIC. Repositorio Institucional del CSIC
Frontiers in Plant Science (5), 1-3. (2014)مصطلحات موضوعية: 0106 biological sciences, Redox signaling, Redox signalling, [SDV]Life Sciences [q-bio], education, Glutaredoxin, Plant Science, Biology, lcsh:Plant culture, Photosynthesis, 01 natural sciences, redox regulation, 03 medical and health sciences, chemistry.chemical_compound, Respiration, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, lcsh:SB1-1110, glutathione, Thioredoxin, redox signaling, homéostasie, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Reactive oxygen species, Vegetal Biology, plants, Editorial Article, thiol, food and beverages, Glutathione, Metabolism, thioredoxin, glutaredoxin, Plants, Biochemistry, chemistry, Redox regulation, plante, Biologie végétale, régulation redox, Homeostasis, 010606 plant biology & botany
وصف الملف: application/pdf
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e08721261c86660d22e70aa1ef5f88bTest
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المؤلفون: Judith Harrison, Karin Groten, Christine H. Foyer, Fabiola Bastian, Mariam Soussi, María Rosario de Felipe, Hélène Vanacker, Raffaella Carzaniga, Alain Puppo, M. Mercedes Lucas
المساهمون: Institut Sophia Agrobiotech [Sophia Antipolis] (ISA), Institut National de la Recherche Agronomique (INRA)-Université Nice Sophia Antipolis (... - 2019) (UNS), Université Côte d'Azur (UCA)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Microbiologie du Sol et de l'Environnement (MSE), Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB), Electron Microscopy Centre, Imperial College London, Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Institut National de la Recherche Agronomique (INRA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11), Institut Sophia Agrobiotech (ISA), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Recherche Agronomique (INRA), Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)
المصدر: New Phytologist
New Phytologist, Wiley, 2005, 165 (3), pp.683-701
Digital.CSIC. Repositorio Institucional del CSIC
instname
New Phytologist, Wiley, 2004, 165 (3), pp.683-701. ⟨10.1111/j.1469-8137.2004.01285.x⟩مصطلحات موضوعية: 0106 biological sciences, Time Factors, Antioxidant, Root nodule, Physiology, medicine.medical_treatment, Apoptosis, Plant Science, medicine.disease_cause, Plant Roots, 01 natural sciences, Antioxidants, chemistry.chemical_compound, Plant Growth Regulators, nodule senescence, cysteine protease, glutathione, Abscisic acid, chemistry.chemical_classification, 0303 health sciences, Fabaceae, Abscisic acid (ABA), Glutathione, Biochemistry, abscisic acid (ABA), Nodule senescence, Signal transduction, Oxidation-Reduction, Signal Transduction, Senescence, Redox signalling, Biology, reactive oxygen species (ROS), 03 medical and health sciences, transcript profiling, medicine, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, Ascorbate, 030304 developmental biology, Reactive oxygen species, Cysteine proteases, Plant Sciences, Reactive oxygen, redox signalling, ascorbate, chemistry, Species (ROS), Transcript profiling, Reactive Oxygen Species, Oxidative stress, 010606 plant biology & botany
الوصف: 23 pages, and figures
Research on legume nodule development has contributed greatly to our current understanding of plant–microbe interactions. However, the factors that orchestrate root nodule senescence have received relatively little attention. Accumulating evidence suggests that redox signals contribute to the establishment of symbiosis and senescence. Although degenerative in nature, nodule senescence is an active process programmed in development in which reactive oxygen species (ROS), antioxidants, hormones and proteinases have key roles. Nodules have high levels of the redox buffers, ascorbate and glutathione, which are important in the nodulation process and in senescence. These metabolites decline with N-fixation as the nodule ages but the resultant decrease in redox buffering capacity does not necessarily lead to enhanced ROS or oxidative stress. We propose models by which ROS and antioxidants interact with hormones such as abscisic acid in the orchestration of nodule senescenceوصف الملف: 610945 bytes; application/pdf; application/octet-stream
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::306c5d7f4273e3f37a4a68df785efda4Test
https://hal.archives-ouvertes.fr/hal-01943161Test -
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المؤلفون: Stéphane D. Lemaire, Jérémy Couturier, Mariette Bedhomme, Christophe H. Marchand, Nicolas Rouhier, Paolo Trost, Mirko Zaffagnini, Mattia Adamo
المساهمون: Dept Expt Evolutionary Biol, Lab Mol Plant Physiol, Alma Mater Studiorum University of Bologna (UNIBO), Biologie moléculaire et cellulaire des eucaryotes, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Ministero dell'Istruzione, dell'Universita e della Ricerca [PRIN2008XB774B-005], ANR (Agence Nationale de la Recherche) [08-BLAN-0153 GLUTAPHOTO, ANR-07-JCJC-0121], PHC (Partenariats Hubert Curien) Galilee Project, Ville de Paris by 'Research in Paris' fellowship, Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Bedhomme M., Adamo M., Marchand Ch., Couturier J., Rouhier N., Lemaire S.D., Zaffagnini M., Trost P.
المصدر: Biochemical Journal
Biochemical Journal, Portland Press, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩
Biochemical Journal, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩مصطلحات موضوعية: Models, Molecular, 0106 biological sciences, REDOX REGULATION, Thioredoxin reductase, [SDV]Life Sciences [q-bio], Arabidopsis, Reductase, YEAST SACCHAROMYCES-CEREVISIAE, BIOTIN-CONJUGATED GLUTATHIONE, 01 natural sciences, Biochemistry, REDUCTASE, chemistry.chemical_compound, Cytosol, Thioredoxins, Glutaredoxin, HYDROGEN PEROXIDE, OXIDATIVE STRESS, Glyceraldehyde 3-phosphate dehydrogenase, chemistry.chemical_classification, 0303 health sciences, REDOX, biology, Glyceraldehyde-3-Phosphate Dehydrogenases, glycolysis, Glutathione, Recombinant Proteins, Amino acid, Isoenzymes, PHOTOSYNTHETIC ORGANISMS, Oxidation-Reduction, EXPRESSION, Thioredoxin-Disulfide Reductase, DNA, Plant, Molecular Sequence Data, PROTEIN S-GLUTATHIONYLATION, Models, Biological, CHLAMYDOMONAS-REINHARDTII, UNIQUE PROPERTIES, 03 medical and health sciences, Amino Acid Sequence, Cysteine, Molecular Biology, Glutaredoxins, 030304 developmental biology, Base Sequence, Sequence Homology, Amino Acid, Arabidopsis Proteins, redox signalling, deglutathionylation, Cell Biology, THIOLATION, Enzyme, chemistry, Mutagenesis, Site-Directed, biology.protein, Arabidopsis thaliana cytosolic isoform I glyceraldehyde-3-phosphate dehydrogenase (AtGapC1), glutathionylation, 010606 plant biology & botany
الوصف: Plants contain both cytosolic and chloroplastic GAPDHs (glyceraldehyde-3-phosphate dehydrogenases). In Arabidopsis thaliana, cytosolic GAPDH is involved in the glycolytic pathway and is represented by two differentially expressed isoforms (GapC1 and GapC2) that are 98% identical in amino acid sequence. In the present study we show that GapC1 is a phosphorylating NAD-specific GAPDH with enzymatic activity strictly dependent on Cys(149). Catalytic Cys(149) is the only solvent-exposed cysteine of the protein and its thiol is relatively acidic (pK(a)=5.7). This property makes GapC1 sensitive to oxidation by H(2)O(2), which appears to inhibit enzyme activity by converting the thiolate of Cys(149) (-S-) into irreversible oxidized forms (-SO(2)(-) and -SO(3)(-)) via a labile sulfenate intermediate (-SO(-)). GSH (reduced glutathione) prevents this irreversible process by reacting with Cys(149) sulfenates to give rise to a mixed disulfide (Cys(149)-SSG), as demonstrated by both MS and biotinylated GSH. Glutathionylated GapC1 can be fully reactivated either by cytosolic glutaredoxin, via a GSH-dependent monothiol mechanism, or, less efficiently, by cytosolic thioredoxins physiologically reduced by NADPH:thioredoxin reductase. The potential relevance of these findings is discussed in the light of the multiple functions of GAPDH in eukaryotic cells (e.g. glycolysis, control of gene expression and apoptosis) that appear to be influenced by the redox state of the catalytic Cys(149).
وصف الملف: STAMPA
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ffeb54a4d7fad0553abbb5b0cd7e466Test
https://hal.archives-ouvertes.fr/hal-01268311Test