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Proc Natl Acad Sci U S A. 2017 Jan 31;114(5):1039-1044. doi: 10.1073/pnas.1615093114. Epub 2017 Jan 17.

TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.

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Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway;
Section for Biochemistry and Molecular Biology, The Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, NO-0371 Oslo, Norway.
Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.
Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway.
Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, NO-0317 Oslo, Norway.


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.


RNA polymerase III; Sumo; TORC1; tRNA; transcription

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