BAIT

ELC1

elongin C, L000004351, YPL046C
Elongin C, conserved among eukaryotes; forms a complex with Cul3p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair
Saccharomyces cerevisiae (S288c)
PREY

CUL3

cullin CUL3, CULLIN B, CULB, YGR003W
Ubiquitin-protein ligase; forms a complex with Elc1p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; cullin family member with similarity to Cdc53p and human CUL3
GO Process (2)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation.

Harreman M, Taschner M, Sigurdsson S, Anindya R, Reid J, Somesh B, Kong SE, Banks CA, Conaway RC, Conaway JW, Svejstrup JQ

The proteasome degrades proteins modified by polyubiquitylation, so correctly controlled ubiquitylation is crucial to avoid unscheduled proteolysis of essential proteins. The mechanism regulating proteolysis of RNAPII has been controversial since two distinct ubiquitin ligases (E3s), Rsp5 (and its human homologue NEDD4) and Elongin-Cullin complex, have both been shown to be required for its DNA-damage-induced polyubiquitylation. Here we show that these ... [more]

Proc. Natl. Acad. Sci. U.S.A. Dec. 08, 2009; 106(49);20705-10 [Pubmed: 19920177]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CUL3 ELC1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID