Alcohol dehydrogenase 1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities in Candida albicans

Sa-Ouk Kang; Min-Kyu Kwak

doi:10.1007/s12275-021-0552-7

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Alcohol dehydrogenase 1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities in Candida albicans: Sa-Ouk Kang ¹, Min-Kyu Kwak ²; Journal of Microbiology 2021;59(1):76-91.
DOI: https://doi.org/10.1007/s12275-021-0552-7
Published online: December 23, 2020

¹Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 08826, Republic of Korea, ²Department of Food and Nutrition, Institute of Food and Nutrition Science, Eulji University, Seongnam 13135, Republic of Korea¹Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 08826, Republic of Korea, ²Department of Food and Nutrition, Institute of Food and Nutrition Science, Eulji University, Seongnam 13135, Republic of Korea

Corresponding author: Sa-Ouk Kang , Tel: +82-31-740-7418,
Min-Kyu Kwak , Tel: +82-31-740-7418,

Received: 29 October 2020 • Revised: 9 November 2020 • Accepted: 9 November 2020

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Abstract

Glutathione reductase (Glr1) activity controls cellular glutathione and reactive oxygen species (ROS). We previously demonstrated two predominant methylglyoxal scavengers– NAD(H)-linked methylglyoxal oxidoreductase (Mgd1) and alcohol dehydrogenase 1 (Adh1)–in glutathione-depleted γ- glutamyl cysteinyl synthetase-disrupted Candida albicans. However, experimental evidence for Candida pathophysiology lacking the enzyme activities of Mgd1 and Adh1 on glutathione- dependent redox regulation remains unclear. Herein, we have aimed to demonstrate that glutathione-dependent enzyme activities coupled with cellular ROS changes is regulated by methylglyoxal accumulation in Δmgd1/Δadh1 double disruptants. Δmgd1/Δadh1 showed severe growth defects and G1-phase cell cycle arrest. The observed complementary and reciprocal methylglyoxal-oxidizing and methylglyoxalreducing activities between Δmgd1 and Δadh1 were not always exhibited in Δmgd1/Δadh1. Although intracellular accumulation of methylglyoxal and pyruvate was shown in all disruptants, to a greater or lesser degree, methylglyoxal was particularly accumulated in the Δmgd1/Δadh1 double disruptant. While cellular ROS significantly increased in Δmgd1 and Δadh1 as compared to the wild-type, Δmgd1/Δadh1 underwent a decrease in ROS in contrast to Δadh1. Despite the experimental findings underlining the importance of the undergoing unbalanced redox state of Δmgd1/Δadh1, glutathione- independent antioxidative enzyme activities did not change during proliferation and filamentation. Contrary to the significantly lowered glutathione content and Glr1 enzyme activity, the activity staining-based glutathione peroxidase activities concomitantly increased in this mutant. Additionally, the enhanced GLR1 transcript supported our results in Δmgd1/Δadh1, indicating that deficiencies of both Adh1 and Mgd1 activities stimulate specific glutathione-dependent enzyme activities. This suggests that glutathione-dependent redox regulation is evidently linked to C. albicans pathogenicity under the control of methylglyoxal-scavenging activities.

Keywords: Astaxanthin;Astaxanthin induction;Haematococcus pluvialis;Ultrasonic treatment

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Alcohol dehydrogenase 1 and NAD(H)-linked methylglyoxal oxidoreductase reciprocally regulate glutathione-dependent enzyme activities in Candida albicans

J. Microbiol. 2021;59(1):76-91. Published online December 23, 2020

DOI: https://doi.org/10.1007/s12275-021-0552-7

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