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)

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.

Publication

Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.

Kater L, Wagener N, Berninghausen O, Becker T, Neupert W, Beckmann R

Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding ... [more]

Nat. Struct. Mol. Biol. Feb. 01, 2020; 27(2);142-149 [Pubmed: 31988523]

Throughput

  • Low Throughput

Additional Notes

  • Electron microscopy (EM) structure

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
BCS1 BCS1
Affinity Capture-MS
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.

High-BioGRID
693841

Curated By

  • BioGRID