BAIT

SUP35

GST1, PNM2, SAL3, SUF12, SUP2, SUP36, translation termination factor GTPase eRF3, eRF3, [PSI(+)], [PSI], L000002200, YDR172W
Translation termination factor eRF3; has a role in mRNA deadenylation and decay; altered protein conformation creates the [PSI(+)] prion that modifies cellular fitness, alters translational fidelity by affecting reading frame selection, and results in a nonsense suppressor phenotype; many stress-response genes are repressed in the presence of [PSI(+)]
GO Process (2)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

REG1

HEX2, PZF240, SPP43, SRN1, protein phosphatase regulator REG1, L000001609, YDR028C
Regulatory subunit of type 1 protein phosphatase Glc7p; involved in negative regulation of glucose-repressible genes; involved in regulation of the nucleocytoplasmic shuttling of Hxk2p; REG1 has a paralog, REG2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae.

Bailleul PA, Newnam GP, Steenbergen JN, Chernoff YO

Striking similarities between cytoskeletal assembly and the "nucleated polymerization" model of prion propagation suggest that similar or overlapping sets of proteins may assist in both processes. We show that the C-terminal domain of the yeast cytoskeletal assembly protein Sla1 (Sla1C) specifically interacts with the N-terminal prion-forming domain (Sup35N) of the yeast release factor Sup35 (eRF3) in the two-hybrid system. Sla1C ... [more]

Genetics Sep. 01, 1999; 153(1);81-94 [Pubmed: 10471702]

Throughput

  • Low Throughput

Curated By

  • BioGRID