NAD-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans |
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| Authors: | Min-Kyu Kwak MyungHee KuSa-Ouk Kang |
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| Affiliation: | Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 151-747, Republic of Korea |
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| Abstract: | We purified a fraction that showed NAD+-linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione-depleted Candida albicans. It also showed NADH-linked methylglyoxal-reducing activity. The fraction was identified as a NAD+-linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1-disruptants of both the wild type and glutathione-depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2-phase arrest was induced. |
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| Keywords: | GCS1, γ-glutamylcysteine synthetase GSH, glutathione MG, methylglyoxal NAD(P)+, nicotinamide adenine dinucleotide (phosphate) NADH, reduced nicotinamide adenine dinucleotide Mgd, methylglyoxal dehydrogenase rpm, revolutions per minute HPLC, high performance liquid chromatography ODS, octadecyl silica PMSF, phenylmethylsulfonyl fluoride FPLC, fast protein liquid chromatography FOA, 5-fluoroorotic acid PMS, phenazine methosulfate MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide PAGE, polyacrylamide gel electrophoresis ADH, alcohol dehydrogenase ORF, open reading frame ROS, reactive oxygen species DCFH-DA, 2&prime ,7&prime -dichlorofluorescein diacetate FACS, fluorescence-activated cell sorting PI, propidium iodide |
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