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Proteomic analysis of boron stress response in yeast saccharomyces cerevisiale
Boron is a versatile element distributed in every part of the environment but most of its deposit reserves are localized in a few countries, Turkey being one of the most prominent. Boron is known to be an essential micronutrient for plants and some animals. Like any other essential element it has toxicity in high concentrations. Herein the mechanism of toxicity and the elements of the boron stress response were investigated in Saccharomyces cerevisiae with a proteomics approach. Boron is believed to have played a role in the evolution of life on earth. It has strongly electrophile organic compounds, the most important physiological form being boric acid. Boric acid has a capacity to bind cis-located hydroxl groups and some amino groups. Some of these groups are located at the active sites of some enzymes and at the carbohydrates with five-membered furanose rings. The riboses of some metabolically important molecules like S-adenosyl methionine, diadenosine phosphate family members and 3'end of RNAs are prone to be affected. The yeast cells subjected to boron in this study expressed higher amounts of carbohydrate metabolic enzymes, proteins involved in protein synthesis, protein folding and catabolism, redox homeostasis and nucleotide synthesis. All of these proteins are common to metal stress responses in yeasts. Some of them involve in other stress responses like peroxide, salt or herbicide stresses showing complex interplay between responses.