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Published on: May 13, 2019
TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity
Pierre Chymkowitch1,2,3, Aurélie Nguéa P4,2,3, Håvard Aanes3
1Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway; jorrit.enserink@rr-research.no pierre.chymkowitch@rr-research.no.
Abstract:
Maintaining cellular homeostasis under changing nutrient conditions is essential for the growth and development of all organisms. The mechanisms that maintain homeostasis upon loss of nutrient supply are not well understood. By mapping the SUMO proteome in Saccharomyces cerevisiae, we discovered a specific set of differentially sumoylated proteins mainly involved in transcription. RNA polymerase III (RNAPIII) components, including Rpc53, Rpc82, and Ret1, are particularly prominent nutrient-dependent SUMO targets. Nitrogen starvation, as well as direct inhibition of the master nutrient response regulator target of rapamycin complex 1 (TORC1), results in rapid desumoylation of these proteins, which is reflected by loss of SUMO at tRNA genes. TORC1-dependent sumoylation of Rpc82 in particular is required for robust tRNA transcription. Mechanistically, sumoylation of Rpc82 is important for assembly of the RNAPIII holoenzyme and recruitment of Rpc82 to tRNA genes. In conclusion, our data show that TORC1-dependent sumoylation of Rpc82 bolsters the transcriptional capacity of RNAPIII under optimal growth conditions.
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