Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.
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 Elongin A ubiquitin ligase and its recruitment ... to sites of DNA damage 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 by DNA-damaging agents and α-amanitin. In addition, we present evidence that the CSB protein promotes stable recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and the CSB protein function together in a common pathway in response to Pol II stalling and DNA damage.
Mesh Terms:
Alpha-Amanitin, Cell Line, Cullin Proteins, DNA Damage, DNA Helicases, DNA Repair, DNA Repair Enzymes, Elongin, Fluorescence Resonance Energy Transfer, Green Fluorescent Proteins, Humans, Image Processing, Computer-Assisted, Mutation, Plasmids, Poly-ADP-Ribose Binding Proteins, RNA Polymerase II, Transcription Factors, Ubiquitin-Protein Ligases
Alpha-Amanitin, Cell Line, Cullin Proteins, DNA Damage, DNA Helicases, DNA Repair, DNA Repair Enzymes, Elongin, Fluorescence Resonance Energy Transfer, Green Fluorescent Proteins, Humans, Image Processing, Computer-Assisted, Mutation, Plasmids, Poly-ADP-Ribose Binding Proteins, RNA Polymerase II, Transcription Factors, Ubiquitin-Protein Ligases
J. Biol. Chem.
Date: Dec. 21, 2016
PubMed ID: 28292928
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