Topological Analysis of the Peripheral Benzodiazepine Receptor in Yeast Mitochondrial Membranes Supports a Five-transmembrane Structure

The peripheral benzodiazepine receptor, implicated in the transport of cholesterol from the outer to the inner mitochondrial membrane, is predicted by hydropathy analysis to feature five membrane-spanning domains, with the amino terminus within the mitochondrial periplasm and the carboxyl terminus i...

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Veröffentlicht in:The Journal of biological chemistry 1998-01, Vol.273 (4), p.2146-2152
Hauptverfasser: Joseph-Liauzun, Evelyne, Delmas, Pascal, Shire, David, Ferrara, Pascual
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Sprache:eng
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Zusammenfassung:The peripheral benzodiazepine receptor, implicated in the transport of cholesterol from the outer to the inner mitochondrial membrane, is predicted by hydropathy analysis to feature five membrane-spanning domains, with the amino terminus within the mitochondrial periplasm and the carboxyl terminus in the external cytoplasm. We have tested these structural predictions directly by immunodetection of c-Myc-tagged peripheral benzodiazepine receptor on intact yeast mitochondria and by specific labeling in yeast membranes of cysteine residues introduced by site-directed mutagenesis. The combined results support the model originally proposed with some minor but important modifications. The theoretical model predicted relatively short α-helical domains, only long enough to span a phospholipid monolayer, whereas the results presented here would support a model with extended α-helices sufficiently long to span an entire membrane bilayer, with concomitant shorter loop and tail regions.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.4.2146