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Title

Protein Carbonylation and Glycation in Legume Nodules

AuthorsMatamoros Galindo, Manuel Ángel ; Kim, Ahyoung; Peñuelas Hortelano, Maria ; Ihling, Christian; Griesser, Eva; Hoffmann, Ralf; Fedorova, Maria; Frolov, Andrej; Becana Ausejo, Manuel
Issue DateAug-2018
PublisherAmerican Society of Plant Biologists
CitationMatamoros MA, Kim A, Peñuelas M, Ihling C, Griesser E, Hoffmann R, Fedorova M, Frolov A, Becana M. Protein Carbonylation and Glycation in Legume Nodules. Plant Physiology 177 (4): 1510–1528 (2018)
AbstractNitrogen 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.
Description19 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.
Publisher version (URL)https://doi.org/10.1104/pp.18.00533
URIhttp://hdl.handle.net/10261/208915
DOIhttps://doi.org/10.1104/pp.18.00533
ISSN0032-0889
E-ISSN1532-2548
Appears in Collections:(EEAD) Artículos
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