Show simple item record

Article

dc.creatorCejudo Fernández, Francisco Javieres
dc.creatorOjeda Servián, Vallees
dc.creatorDelgado Requerey, Victores
dc.creatorPérez Ruiz, Juan Manueles
dc.creatorGonzález García, María de la Cruzes
dc.date.accessioned2019-05-14T07:05:22Z
dc.date.available2019-05-14T07:05:22Z
dc.date.issued2019
dc.identifier.citationCejudo Fernández, F.J., Ojeda Servián, V., Delgado Requerey, V., Pérez Ruiz, J.M. y González García, M.d.l.C. (2019). Chloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darkness. Frontiers in Plant Science, 10 (380), 1-11.
dc.identifier.issn1664-462Xes
dc.identifier.urihttps://hdl.handle.net/11441/86309
dc.description.abstractLight is probably the most important environmental stimulus for plant development. As sessile organisms, plants have developed regulatory mechanisms that allow the rapid adaptation of their metabolism to changes in light availability. Redox regulation based on disulfide-dithiol exchange constitutes a rapid and reversible post-translational modification, which affects protein conformation and activity. This regulatory mechanism was initially discovered in chloroplasts when it was identified that enzymes of the Calvin-Benson cycle (CBC) are reduced and active during the day and become rapidly inactivated by oxidation in the dark. At present, the large number of redox-sensitive proteins identified in chloroplasts extend redox regulation far beyond the CBC. The classic pathway of redox regulation in chloroplasts establishes that ferredoxin (Fdx) reduced by the photosynthetic electron transport chain fuels reducing equivalents to the large set of thioredoxins (Trxs) of this organelle via the activity of a Fdx-dependent Trx reductase (FTR), hence linking redox regulation to light. In addition, chloroplasts harbor an NADPH-dependent Trx reductase with a joint Trx domain, termed NTRC. The presence in chloroplasts of this NADPH-dependent redox system raises the question of the functional relationship between NTRC and the Fdx-FTR-Trx pathways. Here, we update the current knowledge of these two redox systems focusing on recent evidence showing their functional interrelationship through the action of the thiol-dependent peroxidase, 2-Cys peroxiredoxin (2-Cys Prx). The relevant role of 2-Cys Prxs in chloroplast redox homeostasis suggests that hydrogen peroxide may exert a key function to control the redox state of stromal enzymes. Indeed, recent reports have shown the participation of 2-Cys Prxs in enzyme oxidation in the dark, thus providing an explanation for the long-lasting question of photosynthesis deactivation during the light-dark transition.es
dc.description.sponsorshipEspaña, MINECO BIO2017-85195-C2- 1-Pes
dc.description.sponsorshipEspaña, Junta de Andalucía BIO-182es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherFrontiers Mediaes
dc.relation.ispartofFrontiers in Plant Science, 10 (380), 1-11.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectchloroplastes
dc.subjecthydrogen peroxidees
dc.subjectlightes
dc.subjectdarknesses
dc.subjectperoxiredoxines
dc.subjectphotosynthesises
dc.subjectredox regulationes
dc.subjectthioredoxines
dc.titleChloroplast Redox Regulatory Mechanisms in Plant Adaptation to Light and Darknesses
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDBIO-182es
dc.relation.projectIDBIO2017-85195-C2- 1-Pes
dc.relation.publisherversionhttp://dx.doi.org/10.3389/fpls.2019.00380es
dc.identifier.doi10.3389/fpls.2019.00380es
idus.format.extent11 p,es
dc.journaltitleFrontiers in Plant Sciencees
dc.publication.volumen10es
dc.publication.issue380es
dc.publication.initialPage1es
dc.publication.endPage11es

FilesSizeFormatViewDescription
PUBfpls-10-00380.pdf381.0KbIcon   [PDF] View/Open  

This item appears in the following collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as: Attribution-NonCommercial-NoDerivatives 4.0 Internacional