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Vol. 10, Issue 12, 4005-4019, December 1999

Pex17p Is Required for Import of Both Peroxisome Membrane and Lumenal Proteins and Interacts with Pex19p and the Peroxisome Targeting Signal-Receptor Docking Complex in Pichia pastoris

William B. Snyder,* Antonius Koller,* Aaron Jobu Choy,* Monique A. Johnson,dagger James M. Cregg,dagger Linda Rangell,Dagger Gilbert A. Keller,Dagger and Suresh Subramani*§

 *Department of Biology, University of California, San Diego, La Jolla, California 92093-0322;  dagger Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000; and  Dagger Laboratory of Electron Microscopy, Genentech, South San Francisco, California 94080

Pichia pastoris PEX17 was cloned by complementation of a peroxisome-deficient strain obtained from a novel screen for mutants disrupted in the localization of a peroxisomal membrane protein (PMP) reporter. PEX17 encodes a 267-amino-acid protein with low identity (18%) to the previously characterized Saccharomyces cerevisiae Pex17p. Like ScPex17p, PpPex17p contains a putative transmembrane domain near the amino terminus and two carboxyl-terminal coiled-coil regions. PpPex17p behaves as an integral PMP with a cytosolic carboxyl-terminal domain. pex17Delta mutants accumulate peroxisomal matrix proteins and certain integral PMPs in the cytosol, suggesting a critical role for Pex17p in their localization. Peroxisome remnants were observed in the pex17Delta mutant by morphological and biochemical means, suggesting that Pex17p is not absolutely required for remnant formation. Yeast two-hybrid analysis demonstrated that the carboxyl terminus of Pex19p was required for interaction with Pex17p lacking the carboxyl-terminal coiled-coil domains. Biochemical evidence confirmed the interaction between Pex19p and Pex17p. Additionally, Pex17p cross-linked to components of the peroxisome targeting signal-receptor docking complex, which unexpectedly contained Pex3p. Our evidence suggests the existence of distinct subcomplexes that contain separable pools of Pex3p, Pex19p, Pex17p, Pex14p, and the peroxisome targeting signal receptors. These distinct pools may serve different purposes for the import of matrix proteins or PMPs.

§ Corresponding author. E-mail address: ssubramani{at}ucsd.edu.

Molecular Biology of the Cell
Vol. 10, 4005-4019, December 1999
Copyright © 1999 by The American Society for Cell Biology


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