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Molecular and Cellular Biology, October 2004, p. 8895-8906, Vol. 24, No. 20
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.20.8895-8906.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Functional Similarity between the Peroxisomal PTS2 Receptor Binding Protein Pex18p and the N-Terminal Half of the PTS1 Receptor Pex5p

Antje Schäfer,1,{dagger} Daniela Kerssen,1 Marten Veenhuis,2 Wolf-H. Kunau,1 and Wolfgang Schliebs1*

Institut für Physiologische Chemie, Ruhr-Universität Bochum, Bochum, Germany,1 Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands2

Received 2 March 2004/ Returned for modification 1 June 2004/ Accepted 8 July 2004

Within the extended receptor cycle of peroxisomal matrix import, the function of the import receptor Pex5p comprises cargo recognition and transport. While the C-terminal half (Pex5p-C) is responsible for PTS1 binding, the contribution of the N-terminal half of Pex5p (Pex5p-N) to the receptor cycle has been less clear. Here we demonstrate, using different techniques, that in Saccharomyces cerevisiae Pex5p-N alone facilitates the import of the major matrix protein Fox1p. This finding suggests that Pex5p-N is sufficient for receptor docking and cargo transport into peroxisomes. Moreover, we found that Pex5p-N can be functionally replaced by Pex18p, one of two auxiliary proteins of the PTS2 import pathway. A chimeric protein consisting of Pex18p (without its Pex7p binding site) fused to Pex5p-C is able to partially restore PTS1 protein import in a PEX5 deletion strain. On the basis of these results, we propose that the auxiliary proteins of the PTS2 import pathway fulfill roles similar to those of the N-terminal half of Pex5p in the PTS1 import pathway.

* Corresponding author. Mailing address: Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany. Phone: 49-234-32-22033. Fax: 49-234-32-14279. E-mail: wolfgang.schliebs{at}ruhr-uni-bochum.de.

{dagger} Present address: Institut für Biochemie, Universität Stuttgart, D-70569 Stuttgart, Germany.

Molecular and Cellular Biology, October 2004, p. 8895-8906, Vol. 24, No. 20
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.20.8895-8906.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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