Deficiency in frataxin homologue YFH1 in the yeast Pichia guilliermondii leads to missregulation of iron acquisition and riboflavin biosynthesis and affects sulfate assimilation |
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Authors: | Yuriy V Pynyaha Yuriy R Boretsky Daria V Fedorovych Lubov R Fayura Andriy I Levkiv Vira M Ubiyvovk Olha V Protchenko Caroline C Philpott Andriy A Sibirny |
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Institution: | 1. Institute of Cell Biology, NAS of Ukraine, Drahomanov Street 14/16, 79005, Lviv, Ukraine 2. Liver Diseases Branch, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Building 10, Room 9B-16, 10 Center Drive, Bethesda, MD, 20892-1800, USA 3. Rzeszów University, ?wiklińskiej 2, 35-601, Rzeszów, Poland
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Abstract: | Pichia guilliermondii is a representative of yeast species that overproduce riboflavin (vitamin B2) in response to iron deprivation. P. guilliermondii
YFH1 gene coding for frataxin homologue, eukaryotic mitochondrial protein involved in iron trafficking and storage, was identified
and deleted. Constructed P. guilliermondii Δyfh1 mutant grew very poorly in a sucrose-containing synthetic medium supplemented with sulfate or sulfite as a sole sulfur source.
Addition of sodium sulfide, glutathione, cysteine, methionine, N-acetyl-l-cysteine partially restored growth rate of the mutant suggesting that it is impaired in sulfate assimilation. Cellular iron
content in Δyfh1 mutant was ~3–3.5 times higher as compared to the parental strain. It produced 50–70 times more riboflavin in iron sufficient
synthetic media relative to the parental wild-type strain. Biomass yield of the mutant in the synthetic glutathione containing
medium supplemented with glycerol as a sole carbon source was 1.4- and 2.6-fold increased as compared to sucrose and succinate
containing media, respectively. Oxygen uptake of the Δyfh1 mutant on sucrose, glycerol or succinate, when compared to the parental strain, was decreased 5.5-, 1.7- and 1.5-fold, respectively.
Substitution of sucrose or glycerol in the synthetic iron sufficient medium with succinate completely abolished riboflavin
overproduction by the mutants. Deletion of the YFH1 gene caused hypersensitivity to hydrogen peroxide and exogenously added riboflavin and led to alterations in superoxide dismutase
activities. Thus, deletion of the gene coding for yeast frataxin homologue has pleiotropic effect on metabolism in P. guilliermondii. |
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