Pex17p of Saccharomyces cerevisiae Is a Novel Peroxin and Component of the Peroxisomal Protein Translocation Machinery

doi:10.1083/jcb.140.1.49

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© The Rockefeller University Press, 0021-9525/1998//49 $5.00
The Journal of Cell Biology, Volume 140, Number 1, , 1998 49-60

Article

Pex17p of Saccharomyces cerevisiae Is a Novel Peroxin and Component of the Peroxisomal Protein Translocation Machinery

Bettina Huhse, Peter Rehling^*, Markus Albertini^*, Lars Blank^*, Karl Meller, and Wolf-H. Kunau^*

^* Abteilung für Zellbiochemie, Abteilung für Cytologie, Medizinische Fakultät der Ruhr-Universität Bochum, D-44780 Bochum, Germany

The Saccharomyces cerevisiae pex17-1 mutant was isolated froma screen to identify mutants defective in peroxisome biogenesis.pex17-1 and pex17 null mutants fail to import matrix proteinsinto peroxisomes via both PTS1- and PTS2-dependent pathways. The PEX17 gene (formerly PAS9; Albertini, M., P. Rehling, R.Erdmann, W. Girzalsky, J.A.K.W. Kiel, M. Veenhuis, and W.-HKunau. 1997. Cell. 89:83–92) encodes a polypeptide of199 amino acids with one predicted membrane spanning regionand two putative coiled-coil structures. However, localizationstudies demonstrate that Pex17p is a peripheral membrane proteinlocated at the surface of peroxisomes. Particulate structurescontaining the peroxisomal integral membrane proteins Pex3pand Pex11p are evident in pex17 mutant cells, indicating theexistence of peroxisomal remnants ("ghosts"). This finding suggeststhat pex17 null mutant cells are not impaired in peroxisomal membrane biogenesis. Two-hybrid studies showed that Pex17pdirectly binds to Pex14p, the recently proposed point of convergencefor the two peroxisomal targeting signal (PTS)-dependent importpathways, and indirectly to Pex5p, the PTS1 receptor. The latterinteraction requires Pex14p, indicating the potential of these three peroxins to form a trimeric complex. This conclusionis supported by immunoprecipitation experiments showing thatPex14p and Pex17p coprecipitate with both PTS receptors inthe absence of Pex13p. From these and other studies we concludethat Pex17p, in addition to Pex13p and Pex14p, is the third identified component of the peroxisomal translocation machinery.

Abbreviations used in this paper: ORF, open reading frame; PTS, peroxisomal targeting signals.

Bettina Huhse and Peter Rehling both contributed equally tothis manuscript.

Address all correspondence to Prof. Dr. W.-H. Kunau, Abteilung für Zellbiochemie, Medizinische Fakultät, Ruhr-UniversitätBochum, D-44780 Bochum, Germany. Tel.: 0234-7002430. Fax: 0234-7094279.E-mail: Wolf-H.Kunau{at}ruhr-uni-bochum.de

Bettina Huhse's present address is Institute of Cancer Research,Chester Beatty Laboratories, 273 Fulham Road, London, SW3 6JB,UK.

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