Reversal of RNA polymerase II ubiquitylation by the ubiquitin protease Ubp3 Journal Article
| Authors: | Kvint, K.; Uhler, J. P.; Taschner, M. J.; Sigurdsson, S.; Erdjument-Bromage, H.; Tempst, P.; Svejstrup, J. Q. |
| Article Title: | Reversal of RNA polymerase II ubiquitylation by the ubiquitin protease Ubp3 |
| 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. © 2008 Elsevier Inc. All rights reserved. |
| Keywords: | nonhuman; genetic analysis; proteins; cell survival; dna repair; enzyme degradation; gene product; gene function; in vivo study; in vitro study; dna; ubiquitination; saccharomyces cerevisiae; yeast; saccharomyces cerevisiae proteins; ultraviolet rays; rna polymerase ii; enzyme purification; mutant; ultraviolet irradiation; transcriptional elongation factors; endopeptidases; elongation factor; uracil; antimetabolites; def1 protein; spt5 protein; tfiif protein; ubiquitin protease; ubp3 protein |
| Journal Title: | Molecular Cell |
| Volume: | 30 |
| Issue: | 4 |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press |
| Date Published: | 2008-05-23 |
| Start Page: | 498 |
| End Page: | 506 |
| Language: | English |
| DOI: | 10.1016/j.molcel.2008.04.018 |
| PUBMED: | 18498751 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 15" - "Export Date: 17 November 2011" - "CODEN: MOCEF" - "Source: Scopus" |
