- -

Nitric oxide triggers a transient metabolic reprogramming in Arabidopsis

RiuNet: Repositorio Institucional de la Universidad Politécnica de Valencia

Compartir/Enviar a

Citas

Estadísticas

  • Estadisticas de Uso

Nitric oxide triggers a transient metabolic reprogramming in Arabidopsis

Mostrar el registro sencillo del ítem

Ficheros en el ítem

dc.contributor.author Leon Ramos, Jose es_ES
dc.contributor.author Costa-Broseta, Álvaro es_ES
dc.contributor.author Castillo López del Toro, Mª Cruz es_ES
dc.date.accessioned 2017-06-06T09:27:07Z
dc.date.available 2017-06-06T09:27:07Z
dc.date.issued 2016-11-25
dc.identifier.issn 2045-2322
dc.identifier.uri http://hdl.handle.net/10251/82411
dc.description.abstract [EN] Nitric oxide (NO) regulates plant growth and development as well as responses to stress that enhanced its endogenous production. Arabidopsis plants exposed to a pulse of exogenous NO gas were used for untargeted global metabolomic analyses thus allowing the identification of metabolic processes affected by NO. At early time points after treatment, NO scavenged superoxide anion and induced the nitration and the S-nitrosylation of proteins. These events preceded an extensive though transient metabolic reprogramming at 6 h after NO treatment, which included enhanced levels of polyamines, lipid catabolism and accumulation of phospholipids, chlorophyll breakdown, protein and nucleic acid turnover and increased content of sugars. Accordingly, lipid-related structures such as root cell membranes and leaf cuticle altered their permeability upon NO treatment. Besides, NO-treated plants displayed degradation of starch granules, which is consistent with the increased sugar content observed in the metabolomic survey. The metabolic profile was restored to baseline levels at 24 h post-treatment, thus pointing up the plasticity of plant metabolism in response to nitroxidative stress conditions. es_ES
dc.description.sponsorship This work was supported by grants BIO2011-27526 and BIO2014-56067-P from the Spanish Ministry of Economy and Competitiveness and FEDER funds. We thank support and comments from Danny Alexander (Metabolon Inc., USA) on metabolomic analyses. en_EN
dc.language Inglés es_ES
dc.publisher Nature Publishing Group es_ES
dc.relation.ispartof Scientific Reports es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Programmed cell-death es_ES
dc.subject Tyrosine nitration es_ES
dc.subject Abiotic stress es_ES
dc.subject Plant-cells es_ES
dc.subject Posttranslational modification es_ES
dc.subject Clorophyll breakdown es_ES
dc.subject Signaling pathways es_ES
dc.subject Redox balance es_ES
dc.subject Degradation es_ES
dc.subject Responses es_ES
dc.title Nitric oxide triggers a transient metabolic reprogramming in Arabidopsis es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1038/srep37945
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BIO2011-27526/ES/EL OXIDO NITRICO COMO MODULADOR DE LA SEÑALIZACION MEDIADA POR ABA Y GIBERELINAS EN ARABIDOPSIS/ / es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//BIO2014-56067-P/ES/CONTROL DE LA PRODUCCION, PERCEPCION Y SEÑALIZACION DE NO POR MODIFICACIONES POSTRADUCCIONALES Y PROTEOLISIS DIRIGIDA POR LA SECUENCIA AMINOTERMINAL/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes es_ES
dc.description.bibliographicCitation Leon Ramos, J.; Costa-Broseta, Á.; Castillo López Del Toro, MC. (2016). Nitric oxide triggers a transient metabolic reprogramming in Arabidopsis. Scientific Reports. 6:1-14. doi:10.1038/srep37945 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://doi.org/10.1038/srep37945 es_ES
dc.description.upvformatpinicio 1 es_ES
dc.description.upvformatpfin 14 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 6 es_ES
dc.relation.senia 321591 es_ES
dc.identifier.pmid 27885260 en_EN
dc.identifier.pmcid PMC5122866
dc.description.references Arc, E., Galland, M., Godin, B., Cueff, G. & Rajjou, L. Nitric oxide implication in the control of seed dormancy and germination. Front. Plant Sci. 4, 346 (2013). es_ES
dc.description.references Beligni, M. V. & Lamattina, L. Nitric oxide stimulates seed germination and de-etiolation, and inhibits hypocotyl elongation, three light-inducible responses in plants. Planta 210, 215–221 (2000). es_ES
dc.description.references Lozano-Juste, J. & León, J. Nitric oxide regulates DELLA content and PIF expression to promote photomorphogenesis in Arabidopsis. Plant Physiol. 156, 1410–1123 (2011). es_ES
dc.description.references He, Y. et al. Nitric oxide represses the Arabidopsis floral transition. Science 305, 1968–1971 (2004). es_ES
dc.description.references Tsai, Y. C., Delk, N. A., Chowdhury, N. I. & Braam, J. Arabidopsis potential calcium sensors regulate nitric oxide levels and the transition to flowering. Plant Signal. Behav. 2, 446–454 (2007). es_ES
dc.description.references Manjunatha, G., Lokesh, V. & Neelwarne, B. Nitric oxide in fruit ripening: trends and opportunities. Biotechnol. Adv. 28, 489–499 (2010). es_ES
dc.description.references Liu, F. & Guo, F. Q. Nitric oxide deficiency accelerates chlorophyll breakdown and stability loss of thylakoid membranes during dark-induced leaf senescence in Arabidopsis. PLoS One 8(2), e56345 (2013). es_ES
dc.description.references Du, J. et al. Nitric oxide induces cotyledon senescence involving co-operation of the NES1/MAD1 and EIN2-associated ORE1 signalling pathways in Arabidopsis. J. Exp. Bot. 65, 4051–4063 (2014). es_ES
dc.description.references Siddiqui, M. H., Al-Whaibi, M. H. & Basalah, M. O. Role of nitric oxide in tolerance of plants to abiotic stress. Protoplasma 248, 447–455 (2011). es_ES
dc.description.references Arasimowicz-Jelonek, M. & Floryszak-Wieczorek, J. Nitric oxide: an effective weapon of the plant or the pathogen? Mol. Plant Pathol. 15, 406–416 (2014). es_ES
dc.description.references Thomas, D. D. Breathing new life into nitric oxide signaling: A brief overview of the interplay between oxygen and nitric oxide. Redox Biol. 5, 225–33 (2015). es_ES
dc.description.references Groβ, F., Durner, J. & Gaupels, F. Nitric oxide, antioxidants and prooxidants in plant defence responses. Front. Plant Sci. 4, 419 (2013). es_ES
dc.description.references Astier, J. & Lindermayr, C. Nitric oxide-dependent posttranslational modification in plants: an update. Int. J. Mol. Sci. 13, 15193–15208 (2012). es_ES
dc.description.references Hess, D. T. & Stamler, J. S. Regulation by S-nitrosylation of protein post-translational modification. J. Biol. Chem. 287, 4411–4418 (2012). es_ES
dc.description.references Guerra, D. D. & Callis, J. Ubiquitin on the move: the ubiquitin modification system plays diverse roles in the regulation of endoplasmic reticulum- and plasma membrane-localized proteins. Plant Physiol. 160, 56–64 (2012). es_ES
dc.description.references Skalska, K., Miller, J. S. & Ledakowicz, S. Trends in NO(x) abatement: a review. Sci. Total Environ. 408, 3976–3989 (2010). es_ES
dc.description.references Pilegaard, K. Processes regulating nitric oxide emissions from soils. Phil. Transac. Royal Soc. London. Ser. B, Biol. Sci. 368, 20130126 (2013). es_ES
dc.description.references Jaegle, L., Steinberger, L., Martin, R. V. & Chance, K. Global partitioning of NOx sources using satellite observations: Relative roles of fossil fuel combustion, biomass burning and soil emissions. Faraday Discus. 130, 407–423 (2005). es_ES
dc.description.references Gupta, K. J., Fernie, A. R., Kaiser, W. M. & van Dongen, J. T. On the origins of nitric oxide. Trends Plant Sci. 16, 160–168 (2011). es_ES
dc.description.references Mur, L. A. et al. Nitric oxide in plants: an assessment of the current state of knowledge. AoB Plants 5, pls052 (2013). es_ES
dc.description.references Correa-Aragunde, N., Foresi, N. & Lamattina, L. Nitric oxide is a ubiquitous signal for maintaining redox balance in plant cells: regulation of ascorbate peroxidase as a case study. J. Exp. Bot. 66, 2913–2921 (2015). es_ES
dc.description.references Noctor, G., Lelarge-Trouverie, C. & Mhamdi, A. The metabolomics of oxidative stress. Phytochemistry 112, 33–53 (2015). es_ES
dc.description.references Allan, W. L., Simpson, J. P., Clark, S. M. & Shelp, B. J. Gamma-hydroxybutyrate accumulation in Arabidopsis and tobacco plants is a general response to abiotic stress: putative regulation by redox balance and glyoxylate reductase isoforms. J. Exp. Bot. 59, 2555–2564 (2008). es_ES
dc.description.references Romero, L. C., Aroca, M. Á., Laureano-Marín, A. M., Moreno, I., García, I. & Gotor, C. Cysteine and cysteine-related signaling pathways in Arabidopsis thaliana. Mol. Plant 7, 264–276 (2014). es_ES
dc.description.references Noctor, G. et al. Glutathione in plants: an integrated overview. Plant Cell Environ. 35, 454–484 (2012). es_ES
dc.description.references Feussner, I. & Wasternack, C. The lipoxygenase pathway. Ann. Rev. Plant Biol. 53, 275–297 (2002). es_ES
dc.description.references Green, M. A. & Fry, S. C. Vitamin C degradation in plant cells via enzymatic hydrolysis of 4-O-oxalyl-L-threonate. Nature 433, 83–87 (2005). es_ES
dc.description.references Szarka, A., Tomasskovics, B. & Bánhegyi, G. The ascorbate-glutathione-α-tocopherol triad in abiotic stress response. Int. J. Mol. Sci. 13, 4458–4483 (2012). es_ES
dc.description.references Hurlock, A. K., Roston, R. L., Wang, K. & Benning, C. Lipid trafficking in plant cells. Traffic 15, 915–932 (2014). es_ES
dc.description.references Blokhina, O., Virolainen, E. & Fagerstedt, K. V. Antioxidants, oxidative damage and oxygen deprivation stress: a review. Ann. Bot. 91, 179–194 (2003). es_ES
dc.description.references Yeats, T. H. & Rose, J. K. The formation and function of plant cuticles. Plant Physiol. 163, 5–20 (2013). es_ES
dc.description.references Lozano-Juste, J. & León, J. Enhanced abscisic acid-mediated responses in nia1nia2noa1-2 triple mutant impaired in NIA/NR- and AtNOA1-dependent nitric oxide biosynthesis in Arabidopsis. Plant Physiol. 152, 891–903 (2010). es_ES
dc.description.references Hörtensteiner, S. Update on the biochemistry of chlorophyll breakdown. Plant Mol Biol. 82, 505–17 (2013). es_ES
dc.description.references Pruzinská, A. et al. Chlorophyll breakdown in senescent Arabidopsis leaves: characterization of chlorophyll catabolites and of chlorophyll catabolic enzymes involved in the degreening reaction. Plant Physiol. 139, 52–63 (2005). es_ES
dc.description.references Hirashima, M., Tanaka, R. & Tanaka, A. Light-independent cell death induced by accumulation of pheophorbide a in Arabidopsis thaliana. Plant Cell Physiol. 50, 719–29 (2009). es_ES
dc.description.references Zottini, M., Costa, A., De Michele, R., Ruzzene, M., Carimi, F. & Lo Schiavo, F. Salicylic acid activates nitric oxide synthesis in Arabidopsis. J Exp Bot. 58, 1397–1405 (2007). es_ES
dc.description.references Mainz, E. R. et al. Monitoring intracellular nitric oxide production using microchip electrophoresis and laser-induced fluorescence detection. Analytical Methods 4, 414–420 (2012). es_ES
dc.description.references Vandelle, E. & Delledonne, M. Peroxynitrite formation and function in plants. Plant Sci. 181, 534–539 (2011). es_ES
dc.description.references Minocha, R., Majumdar, R. & Minocha, S. C. Polyamines and abiotic stress in plants: a complex relationship. Front. Plant Sci. 5, 175 (2014). es_ES
dc.description.references Parsons H. T., Yasmin, T. & Fry, S. C. Alternative pathways of dehydroascorbic acid degradation in vitro and in plant cell cultures: novel insights into vitamin C catabolism. Biochem. J. 440, 375–383 (2011). es_ES
dc.description.references Hou, Q., Ufer, G. & Bartels, D. Lipid signalling in plant responses to abiotic stress. Plant Cell Environ. 39, 1029–4108 (2016). es_ES
dc.description.references Zhou, X. R., Callahan, D. L., Shrestha, P., Liu, Q., Petrie, J. R. & Singh, S. P. Lipidomic analysis of Arabidopsis seed genetically engineered to contain DHA. Front. Plant Sci. 5, 41 (2014). es_ES
dc.description.references Pohl, C. H. & Kock, J. L. Oxidized fatty acids as inter-kingdom signaling molecules. Molecules 19, 1273–1285 (2014). es_ES
dc.description.references Araújo, W. L., Tohge, T., Ishizaki, K., Leaver, C. J. & Fernie, A. R. Protein degradation-an alternative respiratory substrate for stressed plants. Trends Plant Sci. 16, 489–498 (2011). es_ES
dc.description.references Sakamoto, W. & Takami, T. Nucleases in higher plants and their possible involvement in DNA degradation during leaf senescence. J. Exp. Bot. 65, 3835–3843 (2014). es_ES
dc.description.references Del Duca, S., Serafini-Fracassini, D. & Cai, G. Senescence and programmed cell death in plants: polyamine action mediated by transglutaminase. Front. Plant Sci. 5, 120 (2014). es_ES
dc.description.references Franco, M. C. & Estévez, A. G. Tyrosine nitration as mediator of cell death. Cell. Mol. Life Sci. 71, 3939–3950 (2014). es_ES
dc.description.references Palumbo, A., Fiore, G., Di Cristo, C., Di Cosmo, A. & d’Ischia, M. NMDA receptor stimulation induces temporary alpha-tubulin degradation signalled by nitric oxide-mediated tyrosine nitration in the nervous system of Sepia officinalis. Biochem. Biophys. Res. Commun. 293, 1536–1543 (2002). es_ES
dc.description.references Wang, Y. Y., Lin, S. Y., Chuang, Y. H., Mao, C. H., Tung, K. C. & Sheu, W. H. Protein nitration is associated with increased proteolysis in skeletal muscle of bile duct ligation-induced cirrhotic rats. Metabolism 59, 468–472 (2010). es_ES
dc.description.references Castillo, M. C., Lozano-Juste, J., González-Guzmán, M., Rodriguez, L., Rodriguez, P. L. & León, J. Inactivation of PYR/PYL/RCAR ABA receptors by tyrosine nitration may enable rapid inhibition of ABA signaling by nitric oxide in plants. Sci. Signal. 8(392), ra89 (2015). es_ES
dc.description.references Blaise, G. A., Gauvin, D., Gangal, M. & Authier, S. Nitric oxide, cell signaling and cell death. Toxicology 208, 177–192 (2005). es_ES
dc.description.references Brüne, B. Nitric oxide: NO apoptosis or turning it ON? Cell Death Differ. 10, 864–869 (2003). es_ES
dc.description.references Wang, Y., Chen, C., Loake, G. J. & Chu, C. Nitric oxide: promoter or suppressor of programmed cell death? Prot. Cell 1, 133–142 (2010). es_ES
dc.description.references Serrano, I., Romero-Puertas, M. C., Sandalio, L. M. & Olmedilla, A. The role of reactive oxygen species and nitric oxide in programmed cell death associated with self-incompatibility. J. Exp. Bot. 66, 2869–2876 (2015). es_ES
dc.description.references Huang, S., Hill, R. D. & Stasolla, C. Plant hemoglobin participation in cell fate determination. Plant Signal. Behavior 9, e29485 (2014). es_ES
dc.description.references Maes, M. B., Scharpé, S. & De Meester, I. Dipeptidyl peptidase II (DPPII), a review. Clin. Chim. Acta 380, 31–49 (2007). es_ES
dc.description.references Gibbs, D. J. et al. Nitric oxide sensing in plants is mediated by proteolytic control of group VII ERF transcription factors. Mol. Cell 53, 369–379 (2014). es_ES
dc.description.references Kitamura, K. Inhibition of the Arg/N-end rule pathway-mediated proteolysis by dipeptide-mimetic molecules. Amino Acids 48, 235–243 (2016). es_ES
dc.description.references Duek, P. D., Elmer, M. V., van Oosten, V. R. & Fankhauser C. The degradation of HFR1, a putative bHLH class transcription factor involved in light signaling, is regulated by phosphorylation and requires COP1. Curr Biol. 14, 2296–2301 (2004). es_ES


Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem