BAIT

ELC-1

CELE_Y82E9BR.15, Y82E9BR.15
elc-1 encodes an ortholog of mammalian elongin C that appears to be required for proteolysis of germ plasm components (ZF1-containing proteins) in somatic cells, and for regulation of the cell cycle by CUL-2; elongin C forms a complex with (and positively regulates) elongin A, the active subunit of RNA polymerase II elongation factor SIII, and also binds to the von Hippel-Lindau (VHL) tumor suppressor; in yeast, elongin C also interacts with stress response proteins.
Caenorhabditis elegans

Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

A CUL-2 ubiquitin ligase containing three FEM proteins degrades TRA-1 to regulate C. elegans sex determination.

Starostina NG, Lim JM, Schvarzstein M, Wells L, Spence AM, Kipreos ET

In Caenorhabditis elegans, the Gli-family transcription factor TRA-1 is the terminal effector of the sex-determination pathway. TRA-1 activity inhibits male development and allows female fates. Genetic studies have indicated that TRA-1 is negatively regulated by the fem-1, fem-2, and fem-3 genes. However, the mechanism of this regulation has not been understood. Here, we present data that TRA-1 is regulated by ... [more]

Dev. Cell Jul. 01, 2007; 13(1);127-39 [Pubmed: 17609115]

Throughput

  • Low Throughput

Curated By

  • BioGRID