BAIT

MTQ2

YDR140W
S-adenosylmethionine-dependent methyltransferase; subunit of complex with Trm112p that methylates translation release factor Sup45p (eRF1) in the ternary complex eRF1-eRF3-GTP; similar to E.coli PrmC; member of the seven beta-strand family
GO Process (2)
GO Function (2)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

RTT10

ERE2, TRM734, YPL183C
WD40 domain-containing protein involved in endosomal recycling; forms a complex with Rrt2p that functions in the retromer-mediated pathway for recycling internalized cell-surface proteins; interacts with Trm7p for 2'-O-methylation of N34 of substrate tRNAs; has a role in regulation of Ty1 transposition; human ortholog is WDR6
GO Process (1)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

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 catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.

Lacoux C, Wacheul L, Saraf K, Pythoud N, Huvelle E, Figaro S, Graille M, Carapito C, Lafontaine DLJ, Heurgue-Hamard V

The Mtq2-Trm112 methyltransferase modifies the eukaryotic translation termination factor eRF1 on the glutamine side chain of a universally conserved GGQ motif that is essential for release of newly synthesized peptides. Although this modification is found in the three domains of life, its exact role in eukaryotes remains unknown. As the deletion of MTQ2 leads to severe growth impairment in yeast, ... [more]

Nucleic Acids Res Dec. 02, 2019; 48(21);12310-12325 [Pubmed: 33166396]

Throughput

  • High Throughput

Additional Notes

  • Mtq2-N122

Curated By

  • BioGRID