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Originally published In Press as doi:10.1074/jbc.M106932200 on September 6, 2001

J. Biol. Chem., Vol. 276, Issue 45, 41769-41781, November 9, 2001
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Domain Mapping of Human PEX5 Reveals Functional and Structural Similarities to Saccharomyces cerevisiae Pex18p and Pex21p*

Gabriele DodtDagger §, Daniel Warren, Elisabeth BeckerDagger , Peter Rehling||, and Stephen J. Gould

From the Institut für Physiologische Chemie, Dagger  Systembiochemie Ruhr-Universität, 44801 Bochum, Germany, the  Department of Biological Chemistry, The Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205, and the || Institut für Biochemie und Molekularbiologie, Albert-Ludwigs Universität Freiburg, 79104 Freiburg, Germany

PEX5 functions as an import receptor for proteins with the type-1 peroxisomal targeting signal (PTS1). Although PEX5 is not involved in the import of PTS2-targeted proteins in yeast, it is essential for PTS2 protein import in mammalian cells. Human cells generate two isoforms of PEX5 through alternative splicing, PEX5S and PEX5L, and PEX5L contains an additional insert 37 amino acids long. Only one isoform, PEX5L, is involved in PTS2 protein import, and PEX5L physically interacts with PEX7, the import receptor for PTS2-containing proteins. In this report we map the regions of human PEX5L involved in PTS2 protein import, PEX7 interaction, and targeting to peroxisomes. These studies revealed that amino acids 1-230 of PEX5L are required for PTS2 protein import, amino acids 191-222 are sufficient for PEX7 interaction, and amino acids 1-214 are sufficient for targeting to peroxisomes. We also identified a 21-amino acid-long peptide motif of PEX5L, amino acids 209-229, that overlaps the regions sufficient for full PTS2 rescue activity and PEX7 interaction and is shared by Saccharomyces cerevisiae Pex18p and Pex21p, two yeast peroxins that act only in PTS2 protein import in yeast. A mutation in PEX5 that changes a conserved serine of this motif abrogates PTS2 protein import in mammalian cells and reduces the interaction of PEX5L and PEX7 in vitro. This peptide motif also lies within regions of Pex18p and Pex21p that interact with yeast PEX7. Based on these and other results, we propose that mammalian PEX5L may have acquired some of the functions that yeast Pex18p and/or Pex21p perform in PTS2 protein import. This hypothesis may explain the essential role of PEX5L in PTS2 protein import in mammalian cells and its lack of importance for PTS2 protein import in yeast.

* This work was supported in part by Forschungsförderung Ruhr-Universität Bochum Medìcinische Facultät of the Medizinische Fakultät, Ruhr-Universität Bochum and by the Thyssen Stiftung.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of a Lise Meitner fellowship of the State North Rhine-Wessphalia. To whom correspondence should be addressed: Institut für Physiologische Chemie, Systembiochemie, Ruhr-Universität Bochum, Universitätsstr. 150, Bochum 44801, Germany. Tel.: 49-234-32-24938; Fax: 49-234-32-14279; E-mail: gabriele.dodt@ruhr-uni-bochum.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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