Cockayne syndrome B protein regulates recruitment of the elongin a ubiquitin ligase to sites of DNA damage

Juston C. Weems, Brian D. Slaughter, Jay R. Unruh, Stefan Boeing, Shawn M. Hall, Merry B. McLaird, Takashi Yasukawa, Teijiro Aso, Jesper Q. Svejstrup, Joan W. Conaway, Ronald C. Conaway

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Elongin A performs dual functions as the transcriptionally active subunit of RNA polymerase II (Pol II) elongation factor Elongin and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase that ubiquitylates Pol II in response to DNA damage. Assembly of the ElonginAubiquitin ligase and its recruitment to sites ofDNAdamage is a tightly regulated process induced by DNA-damaging agents and α-Amanitin, a drug that induces Pol II stalling. In this study, we demonstrate (i) that Elongin A and the ubiquitin ligase subunit CUL5 associate in cells with the Cockayne syndrome B (CSB) protein and (ii) that this interaction is also induced byDNA-damagingagentsand α-Amanitin. In addition,we present evidence that theCSBproteinpromotesstable recruitment of the ElonginAubiquitin ligase to sites ofDNAdamage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and theCSBprotein function together in acommonpathway in response to Pol II stalling and DNA damage.

Original languageEnglish (US)
Pages (from-to)6431-6437
Number of pages7
JournalJournal of Biological Chemistry
Issue number16
StatePublished - Apr 21 2017
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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