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Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation

BACKGROUND: 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. Thi...

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Autores principales: Gómez-Pastor, Rocío, Pérez-Torrado, Roberto, Cabiscol, Elisa, Ros, Joaquim, Matallana, Emilia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280929/
https://www.ncbi.nlm.nih.gov/pubmed/22230188
http://dx.doi.org/10.1186/1475-2859-11-4
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author Gómez-Pastor, Rocío
Pérez-Torrado, Roberto
Cabiscol, Elisa
Ros, Joaquim
Matallana, Emilia
author_facet Gómez-Pastor, Rocío
Pérez-Torrado, Roberto
Cabiscol, Elisa
Ros, Joaquim
Matallana, Emilia
author_sort Gómez-Pastor, Rocío
collection PubMed
description BACKGROUND: 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.
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spelling pubmed-32809292012-02-17 Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation Gómez-Pastor, Rocío Pérez-Torrado, Roberto Cabiscol, Elisa Ros, Joaquim Matallana, Emilia Microb Cell Fact Research BACKGROUND: 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. BioMed Central 2012-01-09 /pmc/articles/PMC3280929/ /pubmed/22230188 http://dx.doi.org/10.1186/1475-2859-11-4 Text en Copyright ©2012 Gómez-Pastor et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Gómez-Pastor, Rocío
Pérez-Torrado, Roberto
Cabiscol, Elisa
Ros, Joaquim
Matallana, Emilia
Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title_full Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title_fullStr Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title_full_unstemmed Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title_short Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
title_sort engineered trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280929/
https://www.ncbi.nlm.nih.gov/pubmed/22230188
http://dx.doi.org/10.1186/1475-2859-11-4
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