BAIT

YDR034W-B

Predicted tail-anchored plasma membrane protein; contains conserved CYSTM module; related proteins in other organisms may be involved in response to stress; green fluorescent protein (GFP)-fusion protein localizes to the cell periphery; YDR034W-B has a paralog, YBR056W-A, that arose from the whole genome duplication
GO Process (0)
GO Function (0)
GO Component (0)
Saccharomyces cerevisiae (S288c)
PREY

AKR1

L000000072, YDR264C
Palmitoyl transferase involved in protein palmitoylation; acts as a negative regulator of pheromone response pathway; required for endocytosis of pheromone receptors; involved in cell shape control; contains ankyrin repeats; AKR1 has a paralog, AKR2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Publication

An in vivo map of the yeast protein interactome.

Tarassov K, Messier V, Landry CR, Radinovic S, Serna Molina MM, Shames I, Malitskaya Y, Vogel J, Bussey H, Michnick SW

Protein interactions regulate the systems-level behavior of cells; thus, deciphering the structure and dynamics of protein interaction networks in their cellular context is a central goal in biology. We have performed a genome-wide in vivo screen for protein-protein interactions in Saccharomyces cerevisiae by means of a protein-fragment complementation assay (PCA). We identified 2770 interactions among 1124 endogenously expressed proteins. Comparison ... [more]

Science Jun. 13, 2008; 320(5882);1465-70 [Pubmed: 18467557]

Throughput

  • High Throughput

Curated By

  • BioGRID