DJ-1/ThiJ/PfpI family member proteins play a critical role in the maintenance of mitochondrial integrity and oxidative stress in Saccharomyces cerevisiae
Kondalarao Bankapalli1, Vinaya Vishwanathan1, SreeDivya Saladi1, Divya1 and Patrick D'Silva1* 1Department of Biochemistry, Indian Institute of Science, Bangalore - 560012, India. *Corresponding Author. Mitochondria are essential dynamic organelles, which undergo highly coordinated processes of fusion and fission cycles in the cell. Mitochondrial dynamics is critical for the regulation of several cellular processes, including its life cycle. Previous studies highlight that mutation in ThiJ/DJ-1/PfpI family protein leads to accumulation of dysfunctional mitochondria in the cell. Moreover, loss of DJ-1 members resulted in oxidative stress sensitive altered mitochondrial-dynamics in humans. In the present study, we uncover that yeast Hsp31 (DJ-1 homolog) possesses robust glutathione-independent methylglyoxalase activity and suppresses MG-mediated cytotoxicity and ROS levels in the mitochondrial compartment. In addition, our findings suggest that Hsp31 translocates to the mitochondria and prevent its fragmentation under oxidative stress by redistribution of glutathione (GSH). Furthermore, microscopic analysis reveals significant mitochondrial morphology differences between the deletion of Hsp31 paralogs as compared to WT. Utilizing combined approaches of yeast genetics and biochemical analysis, we reveal that loss of Hsp31 paralogs leads to several morphological defects, including cellular lifespan in yeast. In summary, our findings highlight the importance of DJ-1 family member proteins across the species in the maintenance of mitochondrial integrity, oxidative stress and other critical metabolic pathways.
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