BAIT

TOM22

MAS17, MAS22, MOM22, L000002582, YNL131W
Component of the TOM (Translocase of Outer Membrane) complex; responsible for initial import of mitochondrially directed proteins; mediates interaction between TOM and TIM complexes and acts as a receptor for precursor proteins
Saccharomyces cerevisiae (S288c)
PREY

ELO3

SUR4, APA1, SRE1, VBM1, fatty acid elongase ELO3, L000002245, YLR372W
Elongase; involved in fatty acid and sphingolipid biosynthesis; synthesizes very long chain 20-26-carbon fatty acids from C18-CoA primers; involved in regulation of sphingolipid biosynthesis
GO Process (0)
GO Function (0)
GO Component (0)
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

Recruitment of Cytosolic J-Proteins by TOM Receptors Promotes Mitochondrial Protein Biogenesis.

Opalinski L, Song J, Priesnitz C, Wenz LS, Oeljeklaus S, Warscheid B, Pfanner N, Becker T

Mitochondria possess elaborate machineries for the import of proteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide proteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate for preproteins. How the proteins are delivered to mitochondrial preprotein receptors is poorly understood. We identify the cytosolic J-protein Xdj1 ... [more]

Cell Rep Dec. 20, 2017; 25(8);2036-2043.e5 [Pubmed: 30463002]

Throughput

  • High Throughput

Curated By

  • BioGRID