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Eukaryotic Cell, August 2007, p. 1439-1449, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00084-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Conservation of PEX19-Binding Motifs Required for Protein Targeting to Mammalian Peroxisomal and Trypanosome Glycosomal Membranes ^,

Tracy Saveria,^1,2 André Halbach,³ Ralf Erdmann,³ Rudolf Volkmer-Engert,⁴ Christiane Landgraf,⁴ Hanspeter Rottensteiner,^3, and Marilyn Parsons^1,2,*

Seattle Biomedical Research Institute, Seattle, Washington 98109,¹ University of Washington, Seattle, Washington 98105,² Institut für Physiologische Chemie, Abteilung für Systembiochemie, Ruhr-Universität Bochum, 44801 Bochum, Germany,³ Institut für Medizinische Immunologie, Universitätsklinikum Charité, 10115 Berlin, Germany⁴

Received 15 March 2007/ Accepted 5 June 2007

Glycosomes are divergent peroxisomes found in trypanosomatid protozoa, including those that cause severe human diseases throughout much of the world. While peroxisomes are dispensable for both yeast (Saccharomyces cerevisiae and others) and mammalian cells in vitro, glycosomes are essential for trypanosomes and hence are viewed as a potential drug target. The import of proteins into the matrix of peroxisomes utilizes multiple peroxisomal membrane proteins which require the peroxin PEX19 for insertion into the peroxisomal membrane. In this report, we show that the specificity of peroxisomal membrane protein binding for Trypanosoma brucei PEX19 is very similar to those previously identified for human and yeast PEX19. Our studies show that trafficking is conserved across these distant phyla and that both a PEX19 binding site and a transmembrane domain are required for the insertion of two test proteins into the glycosomal membrane. However, in contrast to T. brucei PEX10 and PEX12, T. brucei PEX14 does not traffic to human peroxisomes, indicating that it is not recognized by the human PEX14 import mechanism.

Published ahead of print on 22 June 2007.

Supplemental material for this article may be found at http://ec.asm.org/.

These authors contributed equally to the manuscript.