Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex.
Bcs1p, a mitochondrial protein and member of the conserved AAA protein family, is involved in the biogenesis of the cytochrome bc(1) complex. We demonstrate here that Bcs1p is directly required for the assembly of the Rieske FeS and Qcr10p proteins into the cytochrome bc(1) complex. Bcs1p binds to a precomplex in the assembly pathway of the cytochrome bc(1) complex. Binding of Bcs1p to and release from this assembly intermediate is driven by ATP hydrolysis. We propose that Bcs1p acts as an ATP-dependent chaperone, maintaining the precomplex in a competent state for the subsequent assembly of the Rieske FeS and Qcr10p proteins.
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Institut für Physiologische Chemie der Universität München, Goethestrasse 33, 80336 München, Germany.
Hell
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Fölsch
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Neupert
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Stuart
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D000255:Adenosine Triphosphate / Q000378:metabolism; D014450:Electron Transport Complex III / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D016296:Mutagenesis; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D007506:Iron-Sulfur Proteins; D018832:Molecular Chaperones; D009687:Nuclear Proteins; C087097:QCR10 protein, S cerevisiae; C037989:Rieske iron-sulfur protein; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; D014450:Electron Transport Complex III