Ubiquitin protease Ubp8 is necessary for S. cerevisiae respiration |
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Authors: | Manuela Leo Giulia Fanelli Serena Di Vito Barbara Traversetti Mariafrancesca La Greca Raffaele A. Palladino Arianna Montanari Silvia Francisci Patrizia Filetici |
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Affiliation: | 1. Dept. of Biology and Biotechnologies “Charles Darwin”, Sapienza University of Rome, P.le A. Moro 5, Rome, Italy;2. Institute of Molecular Biology and Pathology-CNR, Sapienza University of Rome, P.le A. Moro 5, Rome, Italy;3. Pasteur Institute, Cenci Bolognetti Foundation, Italy |
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Abstract: | Healthy mitochondria are required in cell metabolism and deregulation of underlying mechanisms is often involved in human diseases and neurological disorders. Post-translational modifications of mitochondrial proteins regulate their function and activity, accordingly, impairment of ubiquitin proteasome system affects mitochondria homeostasis and organelle dynamics. In the present study we have investigated the role of the ubiquitin protease Ubp8 in S. cerevisiae respiration. We show that Ubp8 is necessary for respiration and its expression is upregulated in glycerol respiratory medium. In addition, we show that the respiratory defects in absence of Ubp8 are efficiently rescued by disruption of the E3 Ub-ligase Psh1, suggesting their epistatic link. Interestingly, we found also that Ubp8 is localized into mitochondria as single protein independently of SAGA complex assembly, thus suggesting an independent function from the nuclear one. We also show evidences on the importance of HAT Gcn5 in sustaining Ubp8 expression and affecting the amount of protein in mitochondria. Collectively, our results have investigated the role of Ubp8 in respiratory metabolism and highlight the role of ubiquitin related pathways in the mitochondrial functions of S. cerevisiae. |
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Keywords: | HAT histone-acetyltransferase Gcn5 General Control Nonderepressible HDAC histone deacetylase CPTH2 cyclopentylidene-[4-(4′-chlorophenyl)thiazol-2-yl)hydrazone Ubp8 ubiquitin protease 8 DUB deubiquitylation Psh1 E3-ubiquitin ligase Ub ubiquitin Por1 porin1 CPTH2 |
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