A recent advance in the intracellular and extracellular redox post-translational modification of proteins in plants

dc.creatorEliel Ruiz May
dc.creatorALDO SEGURA CABRERA
dc.creatorJOSE MIGUEL ELIZALDE CONTRERAS
dc.creatorLaura Shannon
dc.creatorVíctor Manuel Loyola Vargas
dc.date2019
dc.date.accessioned2023-07-21T19:18:41Z
dc.date.available2023-07-21T19:18:41Z
dc.identifierhttp://cicy.repositorioinstitucional.mx/jspui/handle/1003/1564
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7737124
dc.descriptionPlants, as sessile organisms, have acquired through evolution sophisticated regulatory signal pathways to overcome external variable factors during each stage of the life cycle. Among these regulatory signals, two pathways in particular, reactive oxygen species and reactive nitrogen species, have become of significant interest in several aspects of plant biology, underpinning these molecules as critical regulators during development, cellular differentiation, and plant‐pathogen interaction. Recently, redox posttranslational modifications (PTM), such as S‐nitrosylation on cysteine residues and tyrosine nitration, have shed light on multiple protein targets, as they are associated with signal networks/downstream metabolic pathways, capable of transducing the imbalance of redox hemostasis and consequently redirecting the biochemical status under stress conditions. However, most of the redox PTM have been studied only in the intracellular compartment, providing limited information concerning redox PTM in the extracellular matrix of plant cells. Nevertheless, recent studies have indicated the plausibility of redox PTM in extracellular proteins, including cell wall associated proteins. Accordingly, in this review, we endeavor to examine evidence of redox PTM supported by mass spectrometry data in the intracellular and extracellular space in plant cells. As a further example, we focus the last section of this review on illustrating, using molecular dynamics simulation, the effect of S‐nitrosylation on the structural conformation of well‐known cell wall‐associated proteins including pectin methylesterase and xyloglucan endo‐transglycosylases.
dc.formatapplication/pdf
dc.languageeng
dc.relationinfo:eu-repo/semantics/datasetDOI/10.1002/jmr.2754
dc.relationcitation:Ruiz‐May, E., Segura‐Cabrera, A., Elizalde‐Contreras, J. M., Shannon, L. M., & Loyola‐Vargas, V. M. (2019). A recent advance in the intracellular and extracellular redox post‐translational modification of proteins in plants. Journal of Molecular Recognition, 32(1), e2754.
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.sourceJournal of Molecular Recognition, 32(1), e2754, 2019.
dc.subjectinfo:eu-repo/classification/Autores/CELL WALL
dc.subjectinfo:eu-repo/classification/Autores/MOLECULAR DYNAMICS SIMULATION
dc.subjectinfo:eu-repo/classification/Autores/POST‐TRANSLATIONAL MODIFICATIONS
dc.subjectinfo:eu-repo/classification/Autores/PROTEOMICS
dc.subjectinfo:eu-repo/classification/Autores/REACTIVE NITROGEN SPECIES
dc.subjectinfo:eu-repo/classification/cti/2
dc.subjectinfo:eu-repo/classification/cti/2
dc.titleA recent advance in the intracellular and extracellular redox post-translational modification of proteins in plants
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion


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