dc.creator | Garcia, Irene | es |
dc.creator | Arenas Alfonseca, Lucía | es |
dc.creator | Moreno, Inmaculada | es |
dc.creator | Gotor Martínez, Cecilia | es |
dc.creator | Romero González, Luis Carlos | es |
dc.date.accessioned | 2019-03-19T17:38:19Z | |
dc.date.available | 2019-03-19T17:38:19Z | |
dc.date.issued | 2019 | |
dc.identifier.citation | Garcia, I., Arenas Alfonseca, L., Moreno, I., Gotor Martínez, C. y Romero González, L.C. (2019). You have access HCN regulates cellular processes through posttranslational modification of proteins by S-cyanylation. Plant Physiology, 179 (1), 1-36. | |
dc.identifier.issn | 0032-0889 | es |
dc.identifier.uri | https://hdl.handle.net/11441/84405 | |
dc.description.abstract | Hydrogen cyanide (HCN) is coproduced with ethylene in plant cells and is primarily enzymatically detoxified by the mitochondrial β-CYANOALANINE SYNTHASE (CAS-C1). Permanent or transient depletion of CAS-C1 activity in Arabidopsis (Arabidopsis thaliana) results in physiological alterations in the plant that suggest that HCN acts as a gasotransmitter molecule. Label-free quantitative proteomic analysis of mitochondrially enriched samples isolated from the wild type and cas-c1 mutant revealed significant changes in protein content, identifying 451 proteins that are absent or less abundant in cas-c1 and 353 proteins that are only present or more abundant in cas-c1. Gene ontology classification of these proteins identified proteomic changes that explain the root hairless phenotype and the altered immune response observed in the cas-c1 mutant. The mechanism of action of cyanide as a signaling molecule was addressed using two proteomic approaches aimed at identifying the S-cyanylation of Cys as a posttranslational modification of proteins. Both the 2-imino-thiazolidine chemical method and the direct untargeted analysis of proteins using liquid chromatography-tandem mass spectrometry identified a set of 163 proteins susceptible to S-cyanylation that included SEDOHEPTULOSE 1,7-BISPHOSPHATASE (SBPase), the PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 20-3 (CYP20-3), and ENOLASE2 (ENO2). In vitro analysis of these enzymes showed that S-cyanylation of SBPase Cys74, CYP20-3 Cys259, and ENO2 Cys346 residues affected their enzymatic activity. Gene Ontology classification and protein-protein interaction cluster analysis showed that S-cyanylation is involved in the regulation of primary metabolic pathways, such as glycolysis, and the Calvin and S-adenosyl-Met cycles. | es |
dc.description.sponsorship | Agencia Estatal de Investigación BIO2016-76633-P. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society of Plant Biologists | es |
dc.relation.ispartof | Plant Physiology, 179 (1), 1-36. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | You have access HCN regulates cellular processes through posttranslational modification of proteins by S-cyanylation | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/submittedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.projectID | BIO2016-76633-P | es |
dc.relation.publisherversion | https://doi.org/10.1104/pp.18.01083 | es |
dc.identifier.doi | 10.1104/pp.18.01083 | es |
idus.format.extent | 51 | es |
dc.journaltitle | Plant Physiology | es |
dc.publication.volumen | 179 | es |
dc.publication.issue | 1 | es |
dc.publication.initialPage | 1 | es |
dc.publication.endPage | 36 | es |
dc.contributor.funder | Agencia Estatal de Investigación. España | |