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dc.contributor.authorGómez-Pastor, Rocío
dc.contributor.authorPérez-Torrado, Roberto
dc.contributor.authorCabiscol Català, Elisa
dc.contributor.authorRos Salvador, Joaquim
dc.contributor.authorMatallana, Emilia
dc.date.accessioned2012-06-15T11:49:19Z
dc.date.available2012-06-15T11:49:19Z
dc.date.issued2012
dc.identifier.issn1475-2859
dc.identifier.urihttp://hdl.handle.net/10459.1/45585
dc.description.abstractBackground: In the yeast biomass production process, protein carbonylation has severe adverse effects since it diminishes biomass yield and profitability of industrial production plants. However, this significant detriment of yeast performance can be alleviated by increasing thioredoxins levels. Thioredoxins are important antioxidant defenses implicated in many functions in cells, and their primordial functions include scavenging of reactive oxygen species that produce dramatic and irreversible alterations such as protein carbonylation. Results: In this work we have found several proteins specifically protected by yeast Thioredoxin 2 (Trx2p). Bidimensional electrophoresis and carbonylated protein identification from TRX-deficient and TRX-overexpressing cells revealed that glycolysis and fermentation-related proteins are specific targets of Trx2p protection. Indeed, the TRX2 overexpressing strain presented increased activity of the central carbon metabolism enzymes. Interestingly, Trx2p specifically preserved alcohol dehydrogenase I (Adh1p) from carbonylation, decreased oligomer aggregates and increased its enzymatic activity. Conclusions: The identified proteins suggest that the fermentative capacity detriment observed under industrial conditions in T73 wine commercial strain results from the oxidative carbonylation of specific glycolytic and fermentation enzymes. Indeed, increased thioredoxin levels enhance the performance of key fermentation enzymes such as Adh1p, which consequently increases fermentative capacity.ca_ES
dc.description.sponsorshipThis work has been supported by grants AGL 2005-00508 and AGL 2008-00060 from the Spanish Ministry of Education and Science (MEC). R.G-P. was a predoctoral fellow of the I3P program from the CSIC (Spanish National Research Council). R.P-T. was a postdoctoral fellow of the JAEDOC program from the CSIC. We thank the Scientific-Technical Service of Proteomics and Genomics at the University of Lleida for their support in the proteomic analyses.
dc.language.isoengca_ES
dc.publisherBioMed Centralca_ES
dc.relationMIECI/PN2004-2007/AGL 2005-00508
dc.relationMICINN/PN2008-2011/AGL 2008-00060
dc.relation.isformatofReproducció del document publicat a https://doi.org/10.1186/1475-2859-11-4ca_ES
dc.relation.ispartofMicrobial Cell Factories, 2012, vol. 11, núm. 4, p. 1-15ca_ES
dc.rightscc-by, (c) Gómez-Pastor et al., 2012ca_ES
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/es/deed.caca_ES
dc.subjectThioredoxinsca_ES
dc.subjectCarbonylationca_ES
dc.subjectYeastsca_ES
dc.subjectBiomassca_ES
dc.subjectStressca_ES
dc.subject.otherLlevatsca_ES
dc.subject.otherOxidacióca_ES
dc.subject.otherBiomassaca_ES
dc.titleEngineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagationca_ES
dc.typearticleca_ES
dc.identifier.idgrec017591
dc.type.versionpublishedVersionca_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessca_ES
dc.identifier.doihttps://doi.org/10.1186/1475-2859-11-4


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cc-by, (c) Gómez-Pastor et al., 2012
Except where otherwise noted, this item's license is described as cc-by, (c) Gómez-Pastor et al., 2012