Cargando…
Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae
BACKGROUND: Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins are key oxidoreductases which have bee...
Autores principales: | , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836980/ https://www.ncbi.nlm.nih.gov/pubmed/20074363 http://dx.doi.org/10.1186/1471-2091-11-3 |
_version_ | 1782178752155877376 |
---|---|
author | Greetham, Darren Vickerstaff, Jill Shenton, Daniel Perrone, Gabriel G Dawes, Ian W Grant, Chris M |
author_facet | Greetham, Darren Vickerstaff, Jill Shenton, Daniel Perrone, Gabriel G Dawes, Ian W Grant, Chris M |
author_sort | Greetham, Darren |
collection | PubMed |
description | BACKGROUND: Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins are key oxidoreductases which have been implicated in regulating glutathionylation/deglutathionylation in diverse organisms. Glutaredoxins have been proposed to be the predominant deglutathionylase enzymes in many plant and mammalian species, whereas, thioredoxins have generally been thought to be relatively inefficient in deglutathionylation. RESULTS: We show here that the levels of glutathionylated proteins in yeast are regulated in parallel with the growth cycle, and are maximal during stationary phase growth. This increase in glutathionylation is not a response to increased reactive oxygen species generated from the shift to respiratory metabolism, but appears to be a general response to starvation conditions. Our data indicate that glutathionylation levels are constitutively high in all growth phases in thioredoxin mutants and are unaffected in glutaredoxin mutants. We have confirmed that thioredoxins, but not glutaredoxins, catalyse deglutathionylation of model glutathionylated substrates using purified thioredoxin and glutaredoxin proteins. Furthermore, we show that the deglutathionylase activity of thioredoxins is required to reduce the high levels of glutathionylation in stationary phase cells, which occurs as cells exit stationary phase and resume vegetative growth. CONCLUSIONS: There is increasing evidence that the thioredoxin and glutathione redox systems have overlapping functions and these present data indicate that the thioredoxin system plays a key role in regulating the modification of proteins by the glutathione system. |
format | Text |
id | pubmed-2836980 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28369802010-03-12 Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae Greetham, Darren Vickerstaff, Jill Shenton, Daniel Perrone, Gabriel G Dawes, Ian W Grant, Chris M BMC Biochem Research article BACKGROUND: Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins are key oxidoreductases which have been implicated in regulating glutathionylation/deglutathionylation in diverse organisms. Glutaredoxins have been proposed to be the predominant deglutathionylase enzymes in many plant and mammalian species, whereas, thioredoxins have generally been thought to be relatively inefficient in deglutathionylation. RESULTS: We show here that the levels of glutathionylated proteins in yeast are regulated in parallel with the growth cycle, and are maximal during stationary phase growth. This increase in glutathionylation is not a response to increased reactive oxygen species generated from the shift to respiratory metabolism, but appears to be a general response to starvation conditions. Our data indicate that glutathionylation levels are constitutively high in all growth phases in thioredoxin mutants and are unaffected in glutaredoxin mutants. We have confirmed that thioredoxins, but not glutaredoxins, catalyse deglutathionylation of model glutathionylated substrates using purified thioredoxin and glutaredoxin proteins. Furthermore, we show that the deglutathionylase activity of thioredoxins is required to reduce the high levels of glutathionylation in stationary phase cells, which occurs as cells exit stationary phase and resume vegetative growth. CONCLUSIONS: There is increasing evidence that the thioredoxin and glutathione redox systems have overlapping functions and these present data indicate that the thioredoxin system plays a key role in regulating the modification of proteins by the glutathione system. BioMed Central 2010-01-14 /pmc/articles/PMC2836980/ /pubmed/20074363 http://dx.doi.org/10.1186/1471-2091-11-3 Text en Copyright ©2010 Greetham 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 article Greetham, Darren Vickerstaff, Jill Shenton, Daniel Perrone, Gabriel G Dawes, Ian W Grant, Chris M Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title | Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title_full | Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title_fullStr | Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title_full_unstemmed | Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title_short | Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae |
title_sort | thioredoxins function as deglutathionylase enzymes in the yeast saccharomyces cerevisiae |
topic | Research article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836980/ https://www.ncbi.nlm.nih.gov/pubmed/20074363 http://dx.doi.org/10.1186/1471-2091-11-3 |
work_keys_str_mv | AT greethamdarren thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae AT vickerstaffjill thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae AT shentondaniel thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae AT perronegabrielg thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae AT dawesianw thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae AT grantchrism thioredoxinsfunctionasdeglutathionylaseenzymesintheyeastsaccharomycescerevisiae |