Yeast Ppz1 protein phosphatase toxicity involves the alteration of multiple cellular targets

Diego Velázquez, Marcel Albacar, Chunyi Zhang, Carlos Calafí, María López-Malo, Javier Torres-Torronteras, Ramón Martí, Sergey I. Kovalchuk, Benoit Pinson, Ole N. Jensen, Bertrand Daignan-Fornier, Antonio Casamayor, Joaquín Ariño*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

13 Citations (Scopus)


Control of the protein phosphorylation status is a major mechanism for regulation of cellular processes, and its alteration often lead to functional disorders. Ppz1, a protein phosphatase only found in fungi, is the most toxic protein when overexpressed in Saccharomyces cerevisiae. To investigate the molecular basis of this phenomenon, we carried out combined genome-wide transcriptomic and phosphoproteomic analyses. We have found that Ppz1 overexpression causes major changes in gene expression, affecting ~ 20% of the genome, together with oxidative stress and increase in total adenylate pools. Concurrently, we observe changes in the phosphorylation pattern of near 400 proteins (mainly dephosphorylated), including many proteins involved in mitotic cell cycle and bud emergence, rapid dephosphorylation of Snf1 and its downstream transcription factor Mig1, and phosphorylation of Hog1 and its downstream transcription factor Sko1. Deletion of HOG1 attenuates the growth defect of Ppz1-overexpressing cells, while that of SKO1 aggravates it. Our results demonstrate that Ppz1 overexpression has a widespread impact in the yeast cells and reveals new aspects of the regulation of the cell cycle.

Original languageAmerican English
Article number15613
JournalScientific Reports
Issue number1
Publication statusPublished - 1 Dec 2020


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