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- Conaway, Ronald CRemove Conaway, Ronald C filter
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Keyword
- fluorescence resonance energy transfer (FRET)2
- RNA polymerase II2
- ubiquitin ligase2
- acceptor photobleaching-fluorescence resonance energy transfer1
- AP-FRET1
- ChIP1
- chromatin immunoprecipitation1
- chromatin immunoprecipitation (ChIP)1
- Cockayne syndrome B1
- Cockayne syndrome B (CSB)1
- confocal microscopy1
- CSB1
- dithiothreitol1
- DTT1
- ELOA1
- Elongin1
- Elongin A1
- endoplasmic reticulum1
- endoplasmic reticulum stress (ER stress)1
- ER1
- GB1
- gene body1
- GR1
- RNAPII1
Gene Regulation
2 Results
- Research ArticleOpen Access
A role for the Cockayne Syndrome B (CSB)-Elongin ubiquitin ligase complex in signal-dependent RNA polymerase II transcription
Journal of Biological ChemistryVol. 297Issue 1100862Published online: June 8, 2021- Juston C. Weems
- Brian D. Slaughter
- Jay R. Unruh
- Kyle J. Weaver
- Brandon D. Miller
- Kym M. Delventhal
- and others
Cited in Scopus: 2The Elongin complex was originally identified as an RNA polymerase II (RNAPII) elongation factor and subsequently as the substrate recognition component of a Cullin-RING E3 ubiquitin ligase. More recent evidence indicates that the Elongin ubiquitin ligase assembles with the Cockayne syndrome B helicase (CSB) in response to DNA damage and can target stalled polymerases for ubiquitylation and removal from the genome. In this report, we present evidence that the CSB-Elongin ubiquitin ligase pathway has roles beyond the DNA damage response in the activation of RNAPII-mediated transcription. - Gene RegulationOpen Access
Assembly of the Elongin A Ubiquitin Ligase Is Regulated by Genotoxic and Other Stresses
Journal of Biological ChemistryVol. 290Issue 24p15030–15041Published online: April 15, 2015- Juston C. Weems
- Brian D. Slaughter
- Jay R. Unruh
- Shawn M. Hall
- Merry B. McLaird
- Joshua M. Gilmore
- and others
Cited in Scopus: 16Background: Elongin is both a Pol II elongation factor and part of a ubiquitin ligase targeting stalled Pol II.Results: Elongin ubiquitin ligase assembly is driven by signals that provoke Pol II stalling and/or activate Elongin-dependent transcription.Conclusion: Elongin ligase assembly is a regulated process.Significance: This study provides insight into Elongin ubiquitin ligase functions and general mechanisms of ubiquitin ligase activation.