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J. Biol. Chem., Vol. 279, Issue 45, 46573-46579, November 5, 2004

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The N Terminus of the Peroxisomal Cycling Receptor, Pex5p, Is Required for Redirecting the Peroxisome-associated Peroxin Back to the Cytosol^*

João Costa-Rodrigues¶, Andreia F. Carvalho¶, Alexandra M. Gouveia¶||, Marc Fransen**, Clara Sá-Miranda, and Jorge E. Azevedo

From the Instituto de Biologia Molecular e Celular, Rua do Campo Alegre, 823, 4150-180 Porto, Instituto de Ciências Biomédicas de Abel Salazar, Largo do Professor Abel Salazar, 2, 4099-003 Porto, Portugal, ^**Katholieke Universiteit Leuven, Faculteit Geneeskunde, Departement Moleculaire Celbiologie, Herestraat 49, B-3000 Leuven, Belgium, and Instituto de Genética Médica Jacinto de Magalhães, Praça Pedro Nunes, 88, 4050-466 Porto, Portugal

Most newly synthesized peroxisomal matrix proteins are transported to the organelle by Pex5p, a remarkable multidomain protein involved in an intricate network of transient protein-protein interactions. Presently, our knowledge regarding the structure/function of amino acid residues 118 to the very last residue of mammalian Pex5p is quite vast. Indeed, the cargo-protein receptor domain as well as the binding sites for several peroxins have all been mapped to this region of Pex5p. In contrast, structural/functional data regarding the first 117 amino acid residues of Pex5p are still scarce. Here we show that a truncated Pex5p lacking the first 110 amino acid residues (N110-Pex5p) displays exactly the peroxisomal import properties of the full-length peroxin implying that this N-terminal domain is involved neither in cargo-protein binding nor in the docking/translocation step of the Pex5p-cargo protein complex at the peroxisomal membrane. However, the ATP-dependent export step of N110-Pex5p from the peroxisomal membrane is completely blocked, a phenomenon that was also observed for a Pex5p version lacking just the first 17 amino acid residues but not for a truncated protein comprising amino acid residues 1–324 of Pex5p. By exploring the unique properties of N110-Pex5p, the effect of temperature on the import/export kinetics of Pex5p was characterized. Our data indicate that the export step of Pex5p from the peroxisomal compartment (in contrast with its insertion into the organelle membrane) is highly dependent on the temperature.

Received for publication, June 8, 2004 , and in revised form, August 23, 2004.

^* This work was supported in part by Fundação para a Ciência e Tecnologia and FEDER funds. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Supported by Fundação para a Ciência e Tecnologia, Portugal.

^|| Present address: Faculdade de Farmácia, Universidade do Porto, Rua Aníbal Cunha, 164, 4050-047 Porto, Portugal.

To whom correspondence should be addressed: Instituto de Biologia Molecular e Celular, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal. Tel.: 351-226074900; Fax: 351-226099157; E-mail: jazevedo{at}ibmc.up.pt.

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