BAIT

TOM40

ISP42, MOM38, L000000878, YMR203W
Component of the TOM (translocase of outer membrane) complex; responsible for recognition and initial import steps for all mitochondrially directed proteins; constitutes the core element of the protein conducting pore; pre-Tom40p is phosphorylated by PKA, which impairs its import into mitochondria under non-respiratory conditions
GO Process (1)
GO Function (1)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

AHA1

YDR214W
Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress
GO Process (2)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial ?-barrel proteins.

Jores T, Lawatscheck J, Beke V, Franz-Wachtel M, Yunoki K, Fitzgerald JC, Macek B, Endo T, Kalbacher H, Buchner J, Rapaport D

Mitochondrial ?-barrel proteins are encoded in the nucleus, translated by cytosolic ribosomes, and then imported into the organelle. Recently, a detailed understanding of the intramitochondrial import pathway of ?-barrel proteins was obtained. In contrast, it is still completely unclear how newly synthesized ?-barrel proteins reach the mitochondrial surface in an import-competent conformation. In this study, we show that cytosolic Hsp70 ... [more]

J Cell Biol Sep. 03, 2018; 217(9);3091-3108 [Pubmed: 29930205]

Throughput

  • High Throughput

Curated By

  • BioGRID