BAIT

BCS1

bifunctional AAA family ATPase chaperone/translocase BCS1, L000000164, YDR375C
Protein translocase and chaperone required for Complex III assembly; member of the AAA ATPase family; forms a homo-oligomeric complex in the mitochondrial inner membrane that translocates the C-terminal domain of Rip1p from the matrix across the inner membrane, and then delivers it to an assembly intermediate of respiratory Complex III in an ATP-dependent reaction; also required for assembly of the Qcr10p subunit; mutations in human homolog BCS1L linked to neonatal diseases
Saccharomyces cerevisiae (S288c)
PREY

BCS1

bifunctional AAA family ATPase chaperone/translocase BCS1, L000000164, YDR375C
Protein translocase and chaperone required for Complex III assembly; member of the AAA ATPase family; forms a homo-oligomeric complex in the mitochondrial inner membrane that translocates the C-terminal domain of Rip1p from the matrix across the inner membrane, and then delivers it to an assembly intermediate of respiratory Complex III in an ATP-dependent reaction; also required for assembly of the Qcr10p subunit; mutations in human homolog BCS1L linked to neonatal diseases
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

Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae.

Babu M, Vlasblom J, Pu S, Guo X, Graham C, Bean BD, Burston HE, Vizeacoumar FJ, Snider J, Phanse S, Fong V, Tam YY, Davey M, Hnatshak O, Bajaj N, Chandran S, Punna T, Christopolous C, Wong V, Yu A, Zhong G, Li J, Stagljar I, Conibear E, Wodak SJ, Emili A, Greenblatt JF

Macromolecular assemblies involving membrane proteins (MPs) serve vital biological roles and are prime drug targets in a variety of diseases. Large-scale affinity purification studies of soluble-protein complexes have been accomplished for diverse model organisms, but no global characterization of MP-complex membership has been described so far. Here we report a complete survey of 1,590 putative integral, peripheral and lipid-anchored MPs ... [more]

Nature Sep. 27, 2012; 489(7417);585-9 [Pubmed: 22940862]

Throughput

  • High Throughput

Additional Notes

  • Purification data downloaded from http://wodaklab.org/membrane_web/downloads/Purifications.zip, filtered for LCMS/MS confidence > 90% and MALDI-TOF Z-score > 1.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BCS1 BCS1
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
2900628

Curated By

  • BioGRID