Table of Contents Author Guidelines Submit a Manuscript
Volume 1, Issue 3, Pages 188-200<188::AID-YEA27>3.0.CO;2-E
Research Article

Predicting the Function and Subcellular Location of Caenorhabditis elegans Proteins Similar to Saccharomyces cerevisiae β-Oxidation Enzymes

1Institut für Biochemie und Molekulare Zellbiologie der Universität Wien and Ludwig Boltzmann Forschungsstelle für Biochemie, Vienna Biocenter, Dr Bohrgasse 9, Vienna A-1030, Austria
2Institute of Biochemistry and Molecular Cell Biology, University of Vienna, Vienna Biocenter, Dr Bohrgasse 9, Vienna A-1030, Austria

Received 30 May 2000; Accepted 14 July 2000

Copyright © 2000 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The role of peroxisomal processes in the maintenance of neurons has not been thoroughly investigated. We propose using Caenorhabditis elegans as a model organism for studying the molecular basis underlying neurodegeneration in certain human peroxisomal disorders, e.g. Zellweger syndrome, since the nematode neural network is well characterized and relatively simple in function. Here we have identified C. elegans PEX-5 (C34C6.6) representing the receptor for peroxisomal targeting signal type 1 (PTS1), defective in patients with such disorders. PEX-5 interacted strongly in a two-hybrid assay with Gal4p–SKL, and a screen using PEX-5 identified interaction partners that were predominantly terminated with PTS1 or its variants. A list of C. elegans proteins with similarities to well-characterized yeast β-oxidation enzymes was compiled by homology probing. The possible subcellular localization of these orthologues was predicted using an algorithm based on trafficking signals. Examining the C termini of selected nematode proteins for PTS1 function substantiated predictions made regarding the proteins' peroxisomal location. It is concluded that the eukaryotic PEX5-dependent route for importing PTS1-containing proteins into peroxisomes is conserved in nematodes. C. elegans might emerge as an attractive model system for studying the importance of peroxisomes and affiliated processes in neurodegeneration, and also for studying a β-oxidation process that is potentially compartmentalized in both mitochondria and peroxisomes.