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Vol. 14, Issue 10, 4316-4328, October 2003
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Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany
Submitted March 17, 2003;
Revised June 6, 2003;
Accepted June 10, 2003
Monitoring Editor: Howard Riezman
We describe the isolation and characterization of a homologous pair of proteins, Pex25p (YPL112c) and Pex27p (YOR193w), whose C-termini are similar to the entire Pex11p. All three proteins localize to the peroxisomal membrane and are likely to form homo-oligomers. Deletion of any of the three genes resulted in enlarged peroxisomes as revealed by fluorescence and electron microscopy. The partial growth defect on fatty acids of a pex25
mutant was not exacerbated by the additional deletion of PEX27; however, when PEX11 was deleted on top of that, growth was abolished on all fatty acids. Moreover, a severe peroxisomal protein import defect was observed in the pex11pex25pex27 triple mutant strain. This import defect was also observed when cells were grown on ethanol-containing medium, where peroxisomes are not required, suggesting that the function of the proteins in peroxisome biogenesis exceeds their role in proliferation. When Pex25p was overexpressed in the triple mutant strain, growth on oleic acid was completely restored and a massive proliferation of laminar membranes and peroxisomes was observed. Our data demonstrate that Pex11p, Pex25p, and Pex27p build a family of proteins whose members are required for peroxisome biogenesis and play a role in the regulation of peroxisome size and number.
Abbreviations used: MCFA, medium-chain fatty acids; PTS, peroxisomal targeting signal.
* These authors contributed equally to this work.
Present address: Amersham Bioscience, Freiburg, Germany.
Corresponding author. E-mail address: Ralf.Erdmann{at}ruhruni-bochum.de.
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