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Reversal of RNA polymerase II ubiquitylation by the ubiquitin protease Ubp3.

Journal article
Authors Kristian Kvint
Jay Uhler
Michael J Taschner
Stefan Sigurdsson
Hediye Erdjument-Bromage
Paul Tempst
Jesper Q Svejstrup
Published in Molecular cell
Volume 30
Issue 4
Pages 498-506
ISSN 1097-4164
Publication year 2008
Published at
Pages 498-506
Language en
Links dx.doi.org/10.1016/j.molcel.2008.04...
Keywords Cell Survival, DNA Repair, genetics, RNA Polymerase II, Saccharomyces cerevisiae, Transcriptional Elongation Factors, Ubiquitination
Subject categories Molecular biology, Cell and molecular biology, Molecular biology

Abstract

The final outcome of protein polyubiquitylation is often proteasome-mediated proteolysis, meaning that "proofreading" of ubiquitylation by ubiquitin proteases (UBPs) is crucial. Transcriptional arrest can trigger ubiquitin-mediated proteolysis of RNA polymerase II (RNAPII) so a UBP reversing RNAPII ubiquitylation might be expected. Here, we show that Ubp3 deubiquitylates RNAPII in yeast. Genetic characterization of ubp3 cells is consistent with a role in elongation, and Ubp3 can be purified with RNAPII, Def1, and the elongation factors Spt5 and TFIIF. This Ubp3 complex deubiquitylates both mono- and polyubiquitylated RNAPII in vitro, and ubp3 cells have elevated levels of ubiquitylated RNAPII in vivo. Moreover, RNAPII is degraded faster in a ubp3 mutant after UV irradiation. Problems posed by damage-arrested RNAPII are thought to be resolved either by removing the damage or degrading the polymerase. In agreement with this, cells with compromised DNA repair are better equipped to survive UV damage when UPB3 is deleted.

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