Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase
Copper-zinc superoxide dismutase (SOD1) is an antioxidant enzyme that catalyzes the disproportionation of superoxide anion to hydrogen peroxide and molecular oxygen (dioxygen). The yeast <i>Saccharomyces cerevisiae</i> lacking <i>SOD1</i> (Δ<i>sod1</i>) is hyperse...
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author | Magdalena Kwolek-Mirek Aleksandra Dubicka-Lisowska Sabina Bednarska Renata Zadrag-Tecza Pawel Kaszycki |
author_facet | Magdalena Kwolek-Mirek Aleksandra Dubicka-Lisowska Sabina Bednarska Renata Zadrag-Tecza Pawel Kaszycki |
author_sort | Magdalena Kwolek-Mirek |
collection | DOAJ |
description | Copper-zinc superoxide dismutase (SOD1) is an antioxidant enzyme that catalyzes the disproportionation of superoxide anion to hydrogen peroxide and molecular oxygen (dioxygen). The yeast <i>Saccharomyces cerevisiae</i> lacking <i>SOD1</i> (Δ<i>sod1</i>) is hypersensitive to the superoxide anion and displays a number of oxidative stress-related alterations in its phenotype. We compared proteomes of the wild-type strain and the Δ<i>sod1</i> mutant employing two-dimensional gel electrophoresis and detected eighteen spots representing differentially expressed proteins, of which fourteen were downregulated and four upregulated. Mass spectrometry-based identification enabled the division of these proteins into functional classes related to carbon metabolism, amino acid and protein biosynthesis, nucleotide biosynthesis, and metabolism, as well as antioxidant processes. Detailed analysis of the proteomic data made it possible to account for several important morphological, biochemical, and physiological changes earlier observed for the <i>SOD1</i> mutation. An example may be the proposed additional explanation for methionine auxotrophy. It is concluded that protein comparative profiling of the Δ<i>sod1</i> yeast may serve as an efficient tool in the elucidation of the mutation-based systemic alterations in the resultant <i>S. cerevisiae</i> phenotype. |
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language | English |
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spelling | doaj.art-608c08f804c44d0e95b3c414d36ab4962023-11-17T12:37:46ZengMDPI AGMetabolites2218-19892023-03-0113345910.3390/metabo13030459Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide DismutaseMagdalena Kwolek-Mirek0Aleksandra Dubicka-Lisowska1Sabina Bednarska2Renata Zadrag-Tecza3Pawel Kaszycki4Department of Biology, Institute of Biology and Biotechnology, College of Natural Sciences, University of Rzeszow, 35-601 Rzeszow, PolandDepartment of Plant Biology and Biotechnology, Faculty of Biotechnology and Horticulture, University of Agriculture in Krakow, 31-425 Krakow, PolandDepartment of Biology, Institute of Biology and Biotechnology, College of Natural Sciences, University of Rzeszow, 35-601 Rzeszow, PolandDepartment of Biology, Institute of Biology and Biotechnology, College of Natural Sciences, University of Rzeszow, 35-601 Rzeszow, PolandDepartment of Plant Biology and Biotechnology, Faculty of Biotechnology and Horticulture, University of Agriculture in Krakow, 31-425 Krakow, PolandCopper-zinc superoxide dismutase (SOD1) is an antioxidant enzyme that catalyzes the disproportionation of superoxide anion to hydrogen peroxide and molecular oxygen (dioxygen). The yeast <i>Saccharomyces cerevisiae</i> lacking <i>SOD1</i> (Δ<i>sod1</i>) is hypersensitive to the superoxide anion and displays a number of oxidative stress-related alterations in its phenotype. We compared proteomes of the wild-type strain and the Δ<i>sod1</i> mutant employing two-dimensional gel electrophoresis and detected eighteen spots representing differentially expressed proteins, of which fourteen were downregulated and four upregulated. Mass spectrometry-based identification enabled the division of these proteins into functional classes related to carbon metabolism, amino acid and protein biosynthesis, nucleotide biosynthesis, and metabolism, as well as antioxidant processes. Detailed analysis of the proteomic data made it possible to account for several important morphological, biochemical, and physiological changes earlier observed for the <i>SOD1</i> mutation. An example may be the proposed additional explanation for methionine auxotrophy. It is concluded that protein comparative profiling of the Δ<i>sod1</i> yeast may serve as an efficient tool in the elucidation of the mutation-based systemic alterations in the resultant <i>S. cerevisiae</i> phenotype.https://www.mdpi.com/2218-1989/13/3/459copper-zinc superoxide dismutasemethionine auxotrophyoxidative stresssuperoxide anionyeastproteome mapping |
spellingShingle | Magdalena Kwolek-Mirek Aleksandra Dubicka-Lisowska Sabina Bednarska Renata Zadrag-Tecza Pawel Kaszycki Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase Metabolites copper-zinc superoxide dismutase methionine auxotrophy oxidative stress superoxide anion yeast proteome mapping |
title | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_full | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_fullStr | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_full_unstemmed | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_short | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast <i>Saccharomyces cerevisiae</i> Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_sort | changes in a protein profile can account for the altered phenotype of the yeast i saccharomyces cerevisiae i mutant lacking the copper zinc superoxide dismutase |
topic | copper-zinc superoxide dismutase methionine auxotrophy oxidative stress superoxide anion yeast proteome mapping |
url | https://www.mdpi.com/2218-1989/13/3/459 |
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