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Vol. 11, Issue 11, 3963-3976, November 2000
Department of Biochemistry, University of Amsterdam, Academic
Medical Center, Meibergdreef 15 1105 AZ Amsterdam, The Netherlands
A number of peroxisome-associated proteins have been described that
are involved in the import of proteins into peroxisomes, among which is
the receptor for peroxisomal targeting signal 1 (PTS1) proteins
Pex5p, the integral membrane protein Pex13p, which contains an Src
homology 3 (SH3) domain, and the peripheral membrane protein Pex14p. In
the yeast Saccharomyces cerevisiae, both Pex5p and
Pex14p are able to bind Pex13p via its SH3 domain. Pex14p contains the
classical SH3 binding motif PXXP, whereas this sequence is absent in
Pex5p. Mutation of the conserved tryptophan in the PXXP binding pocket
of Pex13-SH3 abolished interaction with Pex14p, but did not affect
interaction with Pex5p, suggesting that Pex14p is the classical SH3
domain ligand and that Pex5p binds the SH3 domain in an alternative
way. To identify the SH3 binding site in Pex5p, we screened a randomly
mutagenized PEX5 library for loss of interaction with
Pex13-SH3. Such mutations were all located in a small region in the
N-terminal half of Pex5p. One of the altered residues (F208) was part
of the sequence W204XXQF208, that is conserved
between Pex5 proteins of different species. Site-directed mutagenesis
of Trp204 confirmed the essential role of this motif in recognition of
the SH3 domain. The Pex5p mutants could only partially restore
PTS1-protein import in pex5
cells in vivo. In vitro
binding studies showed that these Pex5p mutants failed to interact with
Pex13-SH3 in the absence of Pex14p, but regained their ability to bind
in the presence of Pex14p, suggesting the formation of a heterotrimeric
complex consisting of Pex5p, Pex14p, and Pex13-SH3. In vivo, these
Pex5p mutants, like wild-type Pex5p, were still found to be associated
with peroxisomes. Taken together, this indicates that in the absence of
Pex13-SH3 interaction, other protein(s) is able to bind Pex5p at the
peroxisome; Pex14p is a likely candidate for this function.
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