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Eukaryotic Cell, June 2009, p. 830-843, Vol. 8, No. 6
1535-9778/09/$08.00+0     doi:10.1128/EC.00024-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Endoplasmic Reticulum-Associated Secretory Proteins Sec20p, Sec39p, and Dsl1p Are Involved in Peroxisome Biogenesis{triangledown}

Ryan J. Perry, Fred D. Mast, and Richard A. Rachubinski*

Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Received 16 January 2009/ Accepted 25 March 2009

Two pathways have been identified for peroxisome formation: (i) growth and division and (ii) de novo synthesis. Recent experiments determined that peroxisomes originate at the endoplasmic reticulum (ER). Although many proteins have been implicated in the peroxisome biogenic program, no proteins in the eukaryotic secretory pathway have been identified as having roles in peroxisome formation. Using the yeast Saccharomyces cerevisiae regulatable Tet promoter Hughes clone collection, we found that repression of the ER-associated secretory proteins Sec20p and Sec39p resulted in mislocalization of the peroxisomal matrix protein chimera Pot1p-green fluorescent protein (GFP) to the cytosol. Likewise, the peroxisomal membrane protein chimera Pex3p-GFP localized to tubular-vesicular structures in cells suppressed for Sec20p, Sec39p, and Dsl1p, which form a complex at the ER. Loss of Sec39p attenuated formation of Pex3p-derived peroxisomal structures following galactose induction of Pex3p-GFP expression from the GAL1 promoter. Expression of Sec20p, Sec39p, and Dsl1p was moderately increased in yeast grown under conditions that proliferate peroxisomes, and Sec20p, Sec39p, and Dsl1p were found to cofractionate with peroxisomes and colocalize with Pex3p-monomeric red fluorescent protein under these conditions. Our results show that SEC20, SEC39, and DSL1 are essential secretory genes involved in the early stages of peroxisome assembly, and this work is the first to identify and characterize an ER-associated secretory machinery involved in peroxisome biogenesis.

* Corresponding author. Mailing address: Department of Cell Biology, University of Alberta, Medical Sciences Building 5-14, Edmonton, Alberta T6G 2H7, Canada. Phone: (780) 492-9868. Fax: (780) 492-9278. E-mail: rick.rachubinski{at}ualberta.ca

{triangledown} Published ahead of print on 3 April 2009.

Eukaryotic Cell, June 2009, p. 830-843, Vol. 8, No. 6
1535-9778/09/$08.00+0     doi:10.1128/EC.00024-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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