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Induction, identification, and cell-free translation of mRNAs coding for peroxisomal proteins in Candida tropicalis

Peroxisomes have been purified from Candida tropicalis grown on oleic acid and shown to be nearly pure by marker enzyme analysis, electron microscopy, and comparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. They contain approximately 20 polypeptides, among which acyl-CoA oxidase,...

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Bibliographic Details
Published in:The Journal of biological chemistry 1986-11, Vol.261 (33), p.15787-15793
Main Authors: Fujiki, Y, Rachubinski, R A, Zentella-Dehesa, A, Lazarow, P B
Format: Article
Language:English
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Summary:Peroxisomes have been purified from Candida tropicalis grown on oleic acid and shown to be nearly pure by marker enzyme analysis, electron microscopy, and comparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. They contain approximately 20 polypeptides, among which acyl-CoA oxidase, trifunctional hydratase-dehydrogenase-epimerase, and catalase have been identified. Rabbit antisera have been elicited that react with these three proteins. When C. tropicalis is grown on alkanes, a dozen mRNAs are strikingly induced. Nine of the 12 induced mRNAs code for polypeptides that comigrate in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with peroxisomal proteins, among which three have been identified immunochemically as the acyl-CoA oxidase, the trifunctional protein, and catalase. These results indicate that some genes coding for peroxisomal proteins are strongly expressed during growth of C. tropicalis on alkanes. The data are consistent with evidence in other species that peroxisomes form by the post-translational incorporation of newly made proteins into pre-existing peroxisomes, generally without proteolytic processing, followed by peroxisome division.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)66788-2