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J Biol Chem. 2019 Nov 1. pii: jbc.RA119.009721. doi: 10.1074/jbc.RA119.009721. [Epub ahead of print]

De-sumoylation of RNA polymerase III lies at the core of the Sumo stress response in yeast.

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Oslo University Hospital, Norway.
Microbiology, Oslo University Hospital, Norway.
Oslo University Hospital and University of Oslo.


Posttranslational modification by small ubiquitin-like modifier (Sumo) regulates many cellular processes, including the adaptive response to various types of stress, referred to as the Sumo stress response (SSR). However, it remains unclear whether the SSR involves a common set of core proteins regardless of the type of stress or whether each particular type of stress induces a stress-specific SSR that targets a unique, largely non-overlapping set of Sumo substrates. In this study, we used mass spectrometry and a gene ontology approach to identify differentially sumoylated proteins during heat stress, hyperosmotic stress, oxidative stress, nitrogen starvation, and DNA alkylation in Saccharomyces cerevisiae cells. Our results indicate that each stress triggers a specific SSR signature centered on proteins involved in transcription, translation, and chromatin regulation. Strikingly, while the various stress-specific SSRs were largely non-overlapping, all types of stress tested here resulted in de-sumoylation of subunits of RNA polymerase III, which correlated with a decrease in tRNA synthesis. We conclude that de-sumoylation and subsequent inhibition of RNA polymerase III constitutes the core of all stress-specific SSRs in yeast.


Nutrient starvation; RNA polymerase III; Saccharomyces cerevisiae; gene regulation; mass spectrometry (MS); post-translational modification (PTM); small ubiquitin-like modifier (SUMO); stress response; transcription regulation; transfer RNA (tRNA)

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