dc.creator | Ojeda Servián, Valle | es |
dc.creator | Pérez Ruiz, Juan Manuel | es |
dc.creator | Cejudo Fernández, Francisco Javier | es |
dc.date.accessioned | 2019-06-03T15:39:30Z | |
dc.date.available | 2019-06-03T15:39:30Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Ojeda Servián, V., Pérez Ruiz, J.M. y Cejudo Fernández, F.J. (2018). The NADPH-Dependent thioredoxin reductase C-2-Cys peroxiredoxin redox system modulates the activity of thioredoxin x in arabidopsis chloroplasts. Plant and Cell Physiology, 59 (10), 2155-2164. | |
dc.identifier.issn | 0032-0781 | es |
dc.identifier.issn | 1471-9053 | es |
dc.identifier.uri | https://hdl.handle.net/11441/87146 | |
dc.description.abstract | The chloroplast redox network is composed of a complex set of thioredoxins (Trxs), reduced by ferredoxin (Fdx) via a Fdx-dependent Trx reductase (FTR), and an NADPH-dependent Trx reductase with a joint Trx domain, NTRC, which efficiently reduces 2-Cys peroxiredoxins (2-Cys Prxs). Recently, it was proposed that the redox balance of 2-Cys Prxs maintains the redox state of f-type Trxs, thus allowing the proper redox regulation of Calvin-Benson cycle enzymes such as fructose 1,6-bisphosphatase (FBPase). Here, we have addressed whether the action of 2-Cys Prxs is also exerted on Trx x. To that end, an Arabidopsis thaliana quadruple mutant, ntrc-trxx-δ "2cp, which is knocked out for NTRC and Trx x, and contains severely decreased levels of 2-Cys Prxs, was generated. In contrast to ntrc-trxx, which showed a severe growth inhibition phenotype and poor photosynthetic performance, the ntrc-trxx-δ "2cp mutant showed a significant recovery of growth rate and photosynthetic efficiency, indicating that the content of 2-Cys Prxs is critical for the performance of plants lacking both NTRC and Trx x. Light-dependent reduction of FBPase was severely impaired in mutant plants lacking NTRC or NTRC plus Trx x, despite the fact that neither NTRC nor Trx x is an effective reductant of this enzyme. However, FBPase reduction was recovered in the ntrc-trxx-δ "2cp mutant. Our results show that the redox balance of 2-Cys Prxs, which is mostly dependent on NTRC, modulates the activity of Trx x in a similar way as f-type Trxs, thus suggesting that the activity of these Trxs is highly interconnected. | es |
dc.description.sponsorship | Ministerio de Economía y Competitividad BIO2017-85195-C2-1- P | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Plant and Cell Physiology, 59 (10), 2155-2164. | |
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 | Chloroplast | es |
dc.subject | Peroxiredoxin | es |
dc.subject | Redox regulation | es |
dc.subject | Thioredoxin | es |
dc.title | The NADPH-Dependent thioredoxin reductase C-2-Cys peroxiredoxin redox system modulates the activity of thioredoxin x in arabidopsis chloroplasts | 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 | BIO2017-85195-C2-1- P | es |
dc.relation.publisherversion | http://dx.doi.org/10.1093/pcp/pcy134 | es |
dc.identifier.doi | 10.1093/pcp/pcy134 | es |
idus.format.extent | 10 p. | es |
dc.journaltitle | Plant and Cell Physiology | es |
dc.publication.volumen | 59 | es |
dc.publication.issue | 10 | es |
dc.publication.initialPage | 2155 | es |
dc.publication.endPage | 2164 | es |