BAIT

YLR053C

Putative protein of unknown function
GO Process (0)
GO Function (0)
GO Component (0)
Saccharomyces cerevisiae (S288c)
PREY

ARG5,6

bifunctional acetylglutamate kinase/N-acetyl-gamma-glutamyl-phosphate reductase, L000000110, YER069W
Acetylglutamate kinase and N-acetyl-gamma-glutamyl-phosphate reductase; N-acetyl-L-glutamate kinase (NAGK) catalyzes the 2nd and N-acetyl-gamma-glutamyl-phosphate reductase (NAGSA), the 3rd step in arginine biosynthesis; synthesized as a precursor which is processed in the mitochondrion to yield mature NAGK and NAGSA; enzymes form a metabolon complex with Arg2p; NAGK C-terminal domain stabilizes the enzymes, slows catalysis and is involved in feed-back inhibition by arginine
GO Process (3)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

The microprotein Nrs1 rewires the G1/S transcriptional machinery during nitrogen limitation in budding yeast.

Tollis S, Singh J, Palou R, Thattikota Y, Ghazal G, Coulombe-Huntington J, Tang X, Moore S, Blake D, Bonneil E, Royer CA, Thibault P, Tyers M

Commitment to cell division at the end of G1 phase, termed Start in the budding yeast Saccharomyces cerevisiae, is strongly influenced by nutrient availability. To identify new dominant activators of Start that might operate under different nutrient conditions, we screened a genome-wide ORF overexpression library for genes that bypass a Start arrest caused by absence of the G1 cyclin Cln3 ... [more]

PLoS Biol Dec. 01, 2021; 20(3);e3001548 [Pubmed: 35239649]

Throughput

  • Low Throughput

Curated By

  • BioGRID