Pex12p of Saccharomyces cerevisiae is a component of a multi-protein complex essential for peroxisomal matrix protein import.

作者: Markus Albertini , Wolfgang Girzalsky , Marten Veenhuis , Wolf-H. Kunau

DOI: 10.1078/0171-9335-00164

关键词: PeroxinRING finger domainPeroxisomal matrixBiologyIntegral membrane proteinPeroxisomePeroxisomal targeting signalSaccharomyces cerevisiaeRing fingerBiochemistry

摘要: Summary We have isolated the Saccharomyces cerevisiae pex12 – 1 mutant from a screen to identify mutants defective in peroxisome biogenesis. The pex12Δ deletion strain fails import peroxisomal matrix proteins through both PTS1 and PTS2 pathway. PEX12 gene was cloned by functional complementation of encodes polypeptide 399 amino acids. Sc Pex12p is orthologous Pex12 other species like its orthologues, S. contains degenerate RING finger domain C3HC4 type essential carboxy-terminus. Localization studies demonstrate that an integral membrane protein, with NH 2 -terminus facing lumen COOH-terminus cytosol. deficient cells retain particular structures contain consistent existence remnants (“ghosts”) null cells. This finding indicates are not impaired In immunoisolation experiments co-purified protein Pex10p, receptor Pex5p docking for at membrane, Pex13p Pex14p. Furthermore, two-hybrid suggest two domains sufficient Pex10p-Pex12p interaction. Our results component translocation machinery proteins.

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