Imaging-based assays for investigating functions of the RNA polymerase II elongation factor Elongin and the Elongin ubiquitin ligase

Juston C. Weems, Jay R. Unruh, Brian D. Slaughter, Ronald C. Conaway, Joan W. Conaway

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Elongin A binds to Elongins B and C to form the RNA polymerase II transcription elongation factor Elongin. It also functions as the substrate recognition subunit of a ubiquitin ligase that is formed by binding of Elongin to Cullin protein CUL5 and RING finger protein RBX2 and that targets RNA polymerase II for ubiquitination. In this article, we describe use of acceptor photobleaching fluorescence resonance energy transfer (AP-FRET) and laser microirradiation-based assays to study regulated assembly of the Elongin ubiquitin ligase and its recruitment to regions of localized DNA damage.

Original languageEnglish (US)
Pages (from-to)157-164
Number of pages8
JournalMethods
Volume159-160
DOIs
StatePublished - Apr 15 2019
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)

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