Kwolek-Mirek Magdalena, Dubicka-Lisowska Aleksandra, Bednarska Sabina, Zadrag-Tecza Renata, Kaszycki Pawel
Department of Biology, Institute of Biology and Biotechnology, College of Natural Sciences, University of Rzeszow, 35-601 Rzeszow, Poland.
Department of Plant Biology and Biotechnology, Faculty of Biotechnology and Horticulture, University of Agriculture in Krakow, 31-425 Krakow, Poland.
Metabolites. 2023 Mar 22;13(3):459. doi: 10.3390/metabo13030459.
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 lacking (Δ) 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 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 mutation. An example may be the proposed additional explanation for methionine auxotrophy. It is concluded that protein comparative profiling of the Δ yeast may serve as an efficient tool in the elucidation of the mutation-based systemic alterations in the resultant phenotype.
铜锌超氧化物歧化酶（SOD1）是一种抗氧化酶，可催化超氧阴离子歧化为过氧化氢和分子氧（双氧）。缺乏该酶的酵母（Δ）对超氧阴离子高度敏感，其表型出现许多与氧化应激相关的改变。我们采用二维凝胶电泳比较了野生型菌株和Δ突变体的蛋白质组，检测到18个代表差异表达蛋白质的斑点，其中14个下调，4个上调。基于质谱的鉴定能够将这些蛋白质分为与碳代谢、氨基酸和蛋白质生物合成、核苷酸生物合成及代谢以及抗氧化过程相关的功能类别。对蛋白质组数据的详细分析使得解释先前观察到的该突变的几个重要形态、生化和生理变化成为可能。一个例子可能是对甲硫氨酸营养缺陷型的额外解释。结论是，对Δ酵母进行蛋白质比较分析可作为阐明基于该突变的最终表型系统性改变的有效工具。
