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Vol. 11, Issue 1, 141-152, January 2000

Mutants of the Yarrowia lipolytica PEX23 Gene Encoding an Integral Peroxisomal Membrane Peroxin Mislocalize Matrix Proteins and Accumulate Vesicles Containing Peroxisomal Matrix and Membrane Proteins

Trevor W. Brown, Vladimir I. Titorenko, and Richard A. Rachubinski*

Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

pex mutants are defective in peroxisome assembly. The mutant strain pex23-1 of the yeast Yarrowia lipolytica lacks morphologically recognizable peroxisomes and mislocalizes all peroxisomal matrix proteins investigated preferentially to the cytosol. pex23 strains accumulate vesicular structures containing both peroxisomal matrix and membrane proteins. The PEX23 gene was isolated by functional complementation of the pex23-1 strain and encodes a protein, Pex23p, of 418 amino acids (47,588 Da). Pex23p exhibits high sequence similarity to two hypothetical proteins of the yeast Saccharomyces cerevisiae. Pex23p is an integral membrane protein of peroxisomes that is completely, or nearly completely, sequestered from the cytosol. Pex23p is detected at low levels in cells grown in medium containing glucose, and its levels are significantly increased by growth in medium containing oleic acid, the metabolism of which requires intact peroxisomes.

* Corresponding author. E-mail address: rick.rachubinski{at}ualberta.ca.

Molecular Biology of the Cell
Vol. 11, 141-152, January 2000
Copyright © 2000 by The American Society for Cell Biology


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