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J Biol Chem, Vol. 274, Issue 9, 5666-5673, February 26, 1999

Recombinant Human Peroxisomal Targeting Signal Receptor PEX5
STRUCTURAL BASIS FOR INTERACTION OF PEX5 WITH PEX14

Wolfgang Schliebs, Jürgen Saidowsky, Bogos Agianian, Gabriele Dodt, Friedrich W. Herberg, and Wolf-H. Kunau

From the Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany and the  European Molecular Biological Laboratory (EMBL) Heidelberg, Meyerhofstr. 1, D-69012 Heidelberg, Germany

Import of matrix proteins into peroxisomes requires two targeting signal-specific import receptors, Pex5p and Pex7p, and their binding partners at the peroxisomal membrane, Pex13p and Pex14p. Several constructs of human PEX5 have been overexpressed and purified by affinity chromatography in order to determine functionally important interactions and provide initial structural information. Sizing chromatography and electron microscopy suggest that the two isoforms of the human PTS1 receptor, PEX5L and PEX5S, form homotetramers. Surface plasmon resonance analysis indicates that PEX5 binds to the N-terminal fragment of PEX14-(1-78) with a very high affinity in the low nanomolar range. Stable complexes between recombinant PEX14-(1-78) and both the full-length and truncated versions of PEX5 were formed in vitro. Analysis of these complexes revealed that PEX5 possesses multiple binding sites for PEX14, which appear to be distributed throughout its N-terminal half. Coincidentally, this part of the molecule is also responsible for oligomerization, whereas the C-terminal half with its seven tetratricopeptide repeats has been reported to bind PTS1-proteins. A pentapeptide motif that is reiterated seven times in PEX5 is proposed as a determinant for the interaction with PEX14.

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