Repositorio de producción científica de la Universidad de Sevilla

Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation

 

Advanced Search
 

Show simple item record

dc.creator Gotor Martínez, Cecilia es
dc.creator Aroca Aguilar, Ángeles es
dc.creator Romero González, Luis Carlos es
dc.date.accessioned 2018-10-31T09:27:25Z
dc.date.available 2018-10-31T09:27:25Z
dc.date.issued 2018
dc.identifier.citation Gotor Martínez, C., Aroca Aguilar, Á. y Romero González, L.C. (2018). Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Frontiers in Plant Science, 9 (1369), 1-8.
dc.identifier.issn 1664-462X es
dc.identifier.uri https://hdl.handle.net/11441/79730
dc.description.abstract Hydrogen sulfide (H2S) has been largely referred as a toxic gas and environmental hazard, but recent years, it has emerged as an important gas-signaling molecule with effects on multiple physiological processes in both animal and plant systems. The regulatory functions of H2S in plants are involved in important processes such as the modulation of defense responses, plant growth and development, and the regulation of senescence and maturation. The main signaling pathway involving sulfide has been proven to be through protein persulfidation (alternatively called S-sulfhydration), in which the thiol group of cysteine (-SH) in proteins is modified into a persulfide group (-SSH). This modification may cause functional changes in protein activities, structures, and subcellular localizations of the target proteins. New shotgun proteomic approaches and bioinformatic analyses have revealed that persulfidated cysteines regulate important biological processes, highlighting their importance in cell signaling, since about one in 20 proteins in Arabidopsis is persulfidated. During oxidative stress, an increased persulfidation has been reported and speculated that persulfidation is the protective mechanism for protein oxidative damage. Nevertheless, cysteine residues are also oxidized to different post-translational modifications such S-nitrosylation or S-sulfenylation, which seems to be interconvertible. Thus, it must imply a tight cysteine redox regulation essential for cell survival. This review is aimed to focus on the current knowledge of protein persulfidation and addresses the regulation mechanisms that are disclosed based on the knowledge from other cysteine modifications. es
dc.description.sponsorship Unión Europea European Regional Development Fund BIO2016-76633-P es
dc.format application/pdf es
dc.language.iso eng es
dc.publisher Frontiers Media es
dc.relation.ispartof Frontiers in Plant Science, 9 (1369), 1-8.
dc.rights Attribution-NonCommercial-NoDerivatives 4.0 Internacional *
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/ *
dc.subject Arabidopsis es
dc.subject cell signaling es
dc.subject cysteine es
dc.subject hydrogen sulfide es
dc.subject persulfidation es
dc.subject post-translational modification es
dc.subject proteomic es
dc.title Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation 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 BIO2016-76633-P es
dc.relation.publisherversion http://dx.doi.org/ 10.3389/fpls.2018.01369 es
dc.identifier.doi 10.3389/fpls.2018.01369 es
idus.format.extent 8 p. es
dc.journaltitle Frontiers in Plant Science es
dc.publication.volumen 9 es
dc.publication.issue 1369 es
dc.publication.initialPage 1 es
dc.publication.endPage 8 es
dc.contributor.funder European Union (UE)
Size: 967.2Kb
Format: PDF

This item appears in the following Collection(s)

Show simple item record