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)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

BRE1

E3 ubiquitin-protein ligase BRE1, YDL074C
E3 ubiquitin ligase; forms heterodimer with Rad6p to monoubiquinate histone H2B-K123, which is required for the subsequent methylation of histone H3-K4 and H3-K79; required for DSBR, transcription, silencing, and checkpoint control; interacts with RNA-binding protein Npl3p, linking histone ubiquitination to mRNA processing; Bre1p-dependent histone ubiquitination promotes pre-mRNA splicing
UPS Project
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