BAIT

GRX3

monothiol glutaredoxin GRX3, S000007444, YDR098C
Glutathione-dependent oxidoreductase; hydroperoxide and superoxide-radical responsive; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; with Grx4p, binds to Aft1p in iron-replete conditions, promoting its dissociation from promoters; evidence exists indicating that the translation start site is not Met1 as currently annotated, but rather Met36; GRX3 has a paralog, GRX4, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

DRE2

YKR071C
Component of the cytosolic Fe-S protein assembly (CIA) machinery; contains an Fe-S cluster that receives electrons from NADPH via the action of Tah18pin an early step in the CIA pathway; ortholog of human Ciapin1; protein abundance increases in response to DNA replication stress
GO Process (1)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Publication

Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2: requirement of Rnr4 and contribution of Grx3/4 and Dre2.

Zhang Y, Liu L, Wu X, An X, Stubbe J, Huang M

The β2 subunit of class Ia ribonucleotide reductase (RNR) contains a diferric tyrosyl radical cofactor (FeIII2-Y·) that is essential for nucleotide reduction. The β2 subunit of Saccharomyces cerevisiae is a heterodimer of Rnr2 (β) and Rnr4 (β'). Although only β is capable of iron binding and Y· formation, cells lacking β' are either dead or exhibit extremely low Y· levels ... [more]

Unknown Sep. 20, 2011; 0(0); [Pubmed: 21931161]

Throughput

  • Low Throughput

Ontology Terms

  • vegetative growth (APO:0000106)

Additional Notes

  • genetic complex
  • loss of Dre2 causes growth defects in a Grx3/Grx4 mutant background

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
GRX3 DRE2
Affinity Capture-MS
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.

High3BioGRID
3613217
GRX3 DRE2
PCA
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.

High-BioGRID
-

Curated By

  • BioGRID