BAIT

YPR010C-A

Putative protein of unknown function; conserved among Saccharomyces sensu stricto species
GO Process (0)
GO Function (0)
GO Component (0)
Saccharomyces cerevisiae (S288c)
PREY

QRI7

L000002654, YDL104C
Protein involved in threonylcarbamoyl adenosine biosynthesis; Sua5p and Qri7p are necessary and sufficient for RNA t6A modification in vitro; highly conserved mitochondrial protein; essential for t6A modification of mitochondrial tRNAs that decode ANN codons; similar to Kae1p and E. coli YgjD, both of which are also required for tRNA t6A modification; when directed to the cytoplasm, complements the essential function of Kae1p in the KEOPS complex
GO Process (2)
GO Function (0)
GO Component (1)
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

Synchronized assembly of the oxidative phosphorylation system controls mitochondrial respiration in yeast.

Moretti-Horten DN, Peselj C, Taskin AA, Myketin L, Schulte U, Einsle O, Drepper F, Luzarowski M, Voegtle FN

Control of protein stoichiometry is essential for cell function. Mitochondrial oxidative phosphorylation (OXPHOS) presents a complex stoichiometric challenge as the ratio of the electron transport chain (ETC) and ATP synthase must be tightly controlled, and assembly requires coordinated integration of proteins encoded in the nuclear and mitochondrial genome. How correct OXPHOS stoichiometry is achieved is unknown. We identify the Mitochondrial ... [more]

Dev Cell Apr. 22, 2024; 59(8);1043-1057.e8 [Pubmed: 38508182]

Throughput

  • High Throughput

Curated By

  • BioGRID