dc.creator | Aroca Aguilar, Ángeles | es |
dc.creator | Benito, Juan M. | es |
dc.creator | Gotor Martínez, Cecilia | es |
dc.creator | Romero González, Luis Carlos | es |
dc.date.accessioned | 2017-12-20T14:29:12Z | |
dc.date.available | 2017-12-20T14:29:12Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Aroca, Á., Benito, J.M., Gotor Martínez, C. y Romero González, L.C. (2017). Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis. Journal of Experimental Botany, 68 (17), 4915-4927. | |
dc.identifier.issn | 0022-0957 | es |
dc.identifier.uri | http://hdl.handle.net/11441/67880 | |
dc.description.abstract | Hydrogen sulfide-mediated signaling pathways regulate many physiological and pathophysiological processes in
mammalian and plant systems. The molecular mechanism by which hydrogen sulfide exerts its action involves the
post-translational modification of cysteine residues to form a persulfidated thiol motif, a process called protein persulfidation.
We have developed a comparative and quantitative proteomic analysis approach for the detection of
endogenous persulfidated proteins in wild-type Arabidopsis and L-CYSTEINE DESULFHYDRASE 1 mutant leaves
using the tag-switch method. The 2015 identified persulfidated proteins were isolated from plants grown under controlled
conditions, and therefore, at least 5% of the entire Arabidopsis proteome may undergo persulfidation under
baseline conditions. Bioinformatic analysis revealed that persulfidated cysteines participate in a wide range of biological
functions, regulating important processes such as carbon metabolism, plant responses to abiotic and biotic
stresses, plant growth and development, and RNA translation. Quantitative analysis in both genetic backgrounds
reveals that protein persulfidation is mainly involved in primary metabolic pathways such as the tricarboxylic acid
cycle, glycolysis, and the Calvin cycle, suggesting that this protein modification is a new regulatory component in
these pathways. | es |
dc.description.sponsorship | España, MINECO BIO2013-44648-P | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Journal of Experimental Botany, 68 (17), 4915-4927. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Cysteine | es |
dc.subject | hydrogen sulfide | es |
dc.subject | mass spectrometry | es |
dc.subject | persulfidation | es |
dc.subject | post-translational modification | es |
dc.subject | proteomics | es |
dc.title | Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | 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 | BIO2013-44648-P | es |
dc.relation.publisherversion | http://dx.doi.org/doi:10.1093/jxb/erx294 | es |
dc.identifier.doi | doi:10.1093/jxb/erx294 | es |
idus.format.extent | 13 p. | es |
dc.journaltitle | Journal of Experimental Botany | es |
dc.publication.volumen | 68 | es |
dc.publication.issue | 17 | es |
dc.publication.initialPage | 4915 | es |
dc.publication.endPage | 4927 | es |
dc.contributor.funder | Ministerio de Economía y Competitividad (MINECO). España | |