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RNA polymerase II degradation in response to rapamycin is not mediated through ubiquitylation

Nathalie Jouvet Jérémie Poschmann 1 Julie Douville Rim Marrakchi 2 Dindial Ramotar
1 ITUN - Institut de transplantation urologie-néphrologie
2 Biochemistry Laboratory, Hedi Chaker Hospital, Sfax, Tunisia.
Abstract : In Saccharomyces cerevisiae, the immunosuppressor rapamycin engenders the degradation of excessive RNA polymerase II leading to growth arrest but the regulation of this process is not known yet. Here, we show that this mechanism is dependent on the peptidyl prolyl cis/trans isomerase Rrd1. Strikingly this degradation is independent of RNA polymerase II polyubiquitylation and does not require the elongation factor Elc1. Our data reveal that there are at least two alternative pathways to degrade RNA polymerase II that depend on different type of stresses.
Keywords : Rapamycin RNA polymerase II degradation Ubiquitylation Peptidyl prolyl isomerase Rrd1
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https://www.hal.inserm.fr/inserm-02454571
Contributor : Sylvie Le Bihan <>
Submitted on : Friday, January 24, 2020 - 4:08:08 PM
Last modification on : Saturday, January 25, 2020 - 1:25:57 AM

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Nathalie Jouvet, Jérémie Poschmann, Julie Douville, Rim Marrakchi, Dindial Ramotar. RNA polymerase II degradation in response to rapamycin is not mediated through ubiquitylation. Biochemical and Biophysical Research Communications, Elsevier, 2011, 413 (2), pp.248-253. ⟨10.1016/j.bbrc.2011.08.079⟩. ⟨inserm-02454571⟩

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