Protein Carbonylation and Glycation in Legume Nodules
| Autor: | María Peñuelas, Manuel Becana, Maria Fedorova, Manuel A. Matamoros, Christian Ihling, Eva Griesser, Ahyoung Kim, Andrej Frolov, Ralf Hoffmann |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España), European Commission, German Research Foundation, Russian Foundation for Basic Research, Matamoros Galindo, Manuel Ángel [0000-0001-5050-8062], Becana Ausejo, Manuel [0000-0002-1083-0804], Matamoros Galindo, Manuel Ángel, Becana Ausejo, Manuel |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
0301 basic medicine Physiology Protein Carbonylation Lysine Plant Science 01 natural sciences Lipid peroxidation 03 medical and health sciences chemistry.chemical_compound Glycation Malate Dehydrogenase Tandem Mass Spectrometry Glutamate synthase Genetics Amino Acids Leghemoglobin Symbiosis Plant Proteins chemistry.chemical_classification Phaseolus biology Chemistry Nuclear Proteins Metabolism Articles Amino acid 030104 developmental biology Biochemistry biology.protein Root Nodules Plant 010606 plant biology & botany Chromatography Liquid |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | 19 Pags.- 2 Tabls.- 11 Figs.- Supp. Data (15 Figs.- 5 Tabls.- 4 DataSets). Copyright © 2018 American Society of Plant Biologists. All rights reserved. Authors cannot archive post-print (ie final draft post-refereeing): Must link to publisher version, toll-free link provided. Nitrogen fixation is an agronomically and environmentally important process catalyzed by bacterial nitrogenase within legume root nodules. These unique symbiotic organs have high metabolic rates and produce large amounts of reactive oxygen species that may modify proteins irreversibly. Here, we examined two types of oxidative posttranslational modifications of nodule proteins: carbonylation, which occurs by direct oxidation of certain amino acids or by interaction with reactive aldehydes arising from cell membrane lipid peroxides; and glycation, which results from the reaction of lysine and arginine residues with reducing sugars or their autooxidation products. We used a strategy based on the enrichment of carbonylated peptides by affinity chromatography followed by liquid chromatography-tandem mass spectrometry to identify 369 oxidized proteins in bean (Phaseolus vulgaris) nodules. Of these, 238 corresponded to plant proteins and 131 to bacterial proteins. Lipid peroxidation products induced most carbonylation sites. This study also revealed that carbonylation has major effects on two key nodule proteins. Metal-catalyzed oxidation caused the inactivation of malate dehydrogenase and the aggregation of leghemoglobin. In addition, numerous glycated proteins were identified in vivo, including three key nodule proteins: sucrose synthase, glutamine synthetase, and glutamate synthase. Label-free quantification identified 10 plant proteins and 18 bacterial proteins as age-specifically glycated. Overall, our results suggest that the selective carbonylation or glycation of crucial proteins involved in nitrogen metabolism, transcriptional regulation, and signaling may constitute a mechanism to control cell metabolism and nodule senescence. This work was supported by the Ministerio de Economía y Competitividad-Fondos Europeos de Desarrollo Regional (grant AGL2014-53717-R to M.A.M. and M.B.), by the German Research Society (grant FR3117/2-1 to A.F. and A.K.), by the Russian Foundation for Basic Research (grant 18-016-00190 to A.F.), by the Deutsche Forschungsgemeinschaft (grant FE-1236/3-1 to M.F.), and by the European Regional Development Fund (European Union and Free State Saxony; grants 100146238 and 100121468 to M.F.). |
| Databáze: | OpenAIRE |
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