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J. Biol. Chem., Vol. 276, Issue 18, 15034-15041, May 4, 2001
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From the Department of Biochemistry, Academic Medical Center,
University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands
We have studied how Pex5p recognizes peroxisomal
targeting signal type 1 (PTS1)-containing proteins. A randomly
mutagenized pex5 library was screened in a two-hybrid setup
for mutations that disrupted the interaction with the PTS1 protein
Mdh3p or for suppressor mutations that could restore the interaction
with Mdh3p containing a mutation in its PTS1. All mutations localized in the tetratricopeptide repeat (TPR) domain of Pex5p. The Pex5p TPR
domain was modeled based on the crystal structure of a related TPR
protein. Mapping of the mutations on this structural model revealed
that some of the loss-of-interaction mutations consisted of
substitutions in
Recognition of Peroxisomal Targeting Signal Type 1 by the Import
Receptor Pex5p*
-helices of TPRs with bulky amino acids, probably
resulting in local misfolding and thereby indirectly preventing binding
of PTS1 proteins. The other loss-of-interaction mutations and most
suppressor mutations localized in short, exposed, intra-repeat loops of
TPR2, TPR3, and TPR6, which are predicted to mediate direct interaction
with PTS1 amino acids. Additional site-directed mutants at conserved
positions in intra-repeat loops underscored the importance of
the loops of TPR2 and TPR3 for PTS1 interaction. Based on the
mutational analysis and the structural model, we put forward a model as
to how PTS1 proteins are selected by Pex5p.
*
This work was supported by the Netherlands Organization for
Scientific Research and European Community Grant BIO4-97-2180.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.
To whom correspondence should be addressed. Tel.: 31-20-5665127;
Fax: 31-20-6915519; E-mail: b.distel@amc.uva.nl.
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