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

doi:10.1016/j.ymeth.2019.02.015

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 journal › Article › peer-review

6 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 language	English (US)
Pages (from-to)	157-164
Number of pages	8
Journal	Methods
Volume	159-160
DOIs	https://doi.org/10.1016/j.ymeth.2019.02.015
State	Published - Apr 15 2019
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology

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

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.",

author = "Weems, {Juston C.} and Unruh, {Jay R.} and Slaughter, {Brian D.} and Conaway, {Ronald C.} and Conaway, {Joan W.}",

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doi = "10.1016/j.ymeth.2019.02.015",

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T1 - Imaging-based assays for investigating functions of the RNA polymerase II elongation factor Elongin and the Elongin ubiquitin ligase

AU - Weems, Juston C.

AU - Unruh, Jay R.

AU - Slaughter, Brian D.

AU - Conaway, Ronald C.

AU - Conaway, Joan W.

PY - 2019/4/15

Y1 - 2019/4/15

N2 - 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.

AB - 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.

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VL - 159-160

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JO - Methods

JF - Methods

ER -

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

Abstract

ASJC Scopus subject areas

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