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Persulfidation proteome reveals the regulation of protein function by hydrogen sulfide in diverse biological processes in Arabidopsis

 

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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
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
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