Cargando…
Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae 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 Saccharomyces cerevisiae lacking SOD1 (Δsod1) is hypersensitive to the superoxide anion and displays a number of...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10056615/ https://www.ncbi.nlm.nih.gov/pubmed/36984899 http://dx.doi.org/10.3390/metabo13030459 |
_version_ | 1785016166079528960 |
---|---|
author | Kwolek-Mirek, Magdalena Dubicka-Lisowska, Aleksandra Bednarska, Sabina Zadrag-Tecza, Renata Kaszycki, Pawel |
author_facet | Kwolek-Mirek, Magdalena Dubicka-Lisowska, Aleksandra Bednarska, Sabina Zadrag-Tecza, Renata Kaszycki, Pawel |
author_sort | Kwolek-Mirek, Magdalena |
collection | PubMed |
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 Saccharomyces cerevisiae lacking SOD1 (Δsod1) 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 Δsod1 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 SOD1 mutation. An example may be the proposed additional explanation for methionine auxotrophy. It is concluded that protein comparative profiling of the Δsod1 yeast may serve as an efficient tool in the elucidation of the mutation-based systemic alterations in the resultant S. cerevisiae phenotype. |
format | Online Article Text |
id | pubmed-10056615 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100566152023-03-30 Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase Kwolek-Mirek, Magdalena Dubicka-Lisowska, Aleksandra Bednarska, Sabina Zadrag-Tecza, Renata Kaszycki, Pawel Metabolites Article 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 Saccharomyces cerevisiae lacking SOD1 (Δsod1) 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 Δsod1 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 SOD1 mutation. An example may be the proposed additional explanation for methionine auxotrophy. It is concluded that protein comparative profiling of the Δsod1 yeast may serve as an efficient tool in the elucidation of the mutation-based systemic alterations in the resultant S. cerevisiae phenotype. MDPI 2023-03-22 /pmc/articles/PMC10056615/ /pubmed/36984899 http://dx.doi.org/10.3390/metabo13030459 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kwolek-Mirek, Magdalena Dubicka-Lisowska, Aleksandra Bednarska, Sabina Zadrag-Tecza, Renata Kaszycki, Pawel Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_full | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_fullStr | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_full_unstemmed | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_short | Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase |
title_sort | changes in a protein profile can account for the altered phenotype of the yeast saccharomyces cerevisiae mutant lacking the copper-zinc superoxide dismutase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10056615/ https://www.ncbi.nlm.nih.gov/pubmed/36984899 http://dx.doi.org/10.3390/metabo13030459 |
work_keys_str_mv | AT kwolekmirekmagdalena changesinaproteinprofilecanaccountforthealteredphenotypeoftheyeastsaccharomycescerevisiaemutantlackingthecopperzincsuperoxidedismutase AT dubickalisowskaaleksandra changesinaproteinprofilecanaccountforthealteredphenotypeoftheyeastsaccharomycescerevisiaemutantlackingthecopperzincsuperoxidedismutase AT bednarskasabina changesinaproteinprofilecanaccountforthealteredphenotypeoftheyeastsaccharomycescerevisiaemutantlackingthecopperzincsuperoxidedismutase AT zadragteczarenata changesinaproteinprofilecanaccountforthealteredphenotypeoftheyeastsaccharomycescerevisiaemutantlackingthecopperzincsuperoxidedismutase AT kaszyckipawel changesinaproteinprofilecanaccountforthealteredphenotypeoftheyeastsaccharomycescerevisiaemutantlackingthecopperzincsuperoxidedismutase |