Respiratory deficient pet mutants of Saccharomyces cerevisiae assigned to complementation group G2 define a new gene, named BCS1, whose product is shown to be necessary for the expression of functional ubiquinol-cytochrome c reductase (bc1) complex. Immunological assays indicate a gross reduction in the Rieske iron-sulfur subunit in bcs1 mutants, while other subunits of the ubiquinol-cytochrome c reductase complex are present at concentrations comparable to the wild type. Transformation of bcs1 mutants with the iron-sulfur protein gene on a multicopy plasmid led to elevated mitochondrial concentrations of Rieske protein, but did not correct the enzymatic defect, indicating that BCS1 is involved either in forming the active site iron-sulfur cluster or providing a chaperone-like function in assembling the Rieske protein with the other subunits of the complex. Both postulated functions are consistent with the localization of BCS1 in mitochondria. To facilitate further studies on this novel protein, BCS1 was cloned by transformation of a bcs1 mutant and its structure determined. The primary structure of the encoded BCS1 protein bears similarity to a group of proteins that have been implicated in intracellular protein sorting, membrane fusion and regulation of transcription. The region of BCS1 homologous to this diverse group of proteins is approximately 200 amino acids long and includes several signature sequences commonly found in ATPases and nucleotide binding proteins.

• PMID: 1327750
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Comparative Study | Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.

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Nobrega FG, Nobrega MP, Tzagoloff A

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