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The Journal of Cell Biology, Vol 135, 97-109, Copyright © 1996 by The Rockefeller University Press
ARTICLES |
Y Elgersma, L Kwast, A Klein, T Voorn-Brouwer, M van den Berg, B Metzig, T America, HF Tabak and B Distel
Department of Biochemistry, Academic Medical Centre, Amsterdam, The Netherlands.
We identified a Saccharomyces cerevisiae peroxisomal membrane protein, Pex13p, that is essential for protein import. A point mutation in the COOH-terminal Src homology 3 (SH3) domain of Pex13p inactivated the protein but did not affect its membrane targeting. A two-hybrid screen with the SH3 domain of Pex13p identified Pex5p, a receptor for proteins with a type I peroxisomal targeting signal (PTS1), as its ligand. Pex13p SH3 interacted specifically with Pex5p in vitro. We determined, furthermore, that Pex5p was mainly present in the cytosol and only a small fraction was associated with peroxisomes. We therefore propose that Pex13p is a component of the peroxisomal protein import machinery onto which the mobile Pex5p receptor docks for the delivery of the selected PTS1 protein.
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