The Hansenula polymorpha peroxisomal targeting signal 1 receptor, Pex5p, functions as a tetramer

• Published in: FEBS letters 2007-05, Vol.581 (9), p.1758-1762
• Main Authors: Moscicka, Katarzyna B., Klompmaker, Sandra H., Wang, Dongyuan, van der Klei, Ida J., Boekema, Egbert J.
• Format: Article
• Language: English
• Subjects: Dimerization; Electron microscopy; Fungal Proteins - chemistry; Fungal Proteins - metabolism; Hansenula polymorpha; Membrane transport; Models, Molecular; Multiprotein Complexes - chemistry; Multiprotein Complexes - metabolism; Peroxisome; Peroxisome-Targeting Signal 1 Receptor; Pex5p; Pichia; Protein Binding; Receptors, Cytoplasmic and Nuclear - chemistry; Receptors, Cytoplasmic and Nuclear - metabolism; Receptors, Cytoplasmic and Nuclear - physiology
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2007.03.061

We have studied Hansenula polymorpha Pex5p and Pex20p, peroxins involved in peroxisomal matrix protein import. In vitro binding experiments suggested that H. polymorpha Pex5p and Pex20p physically interact. We used single particle electron microscopy (EM) to analyze the structure of purified Pex5p and its possible association with Pex20p. Upon addition of Pex20p, a multimeric Pex20p complex was observed to be associated to the periphery of the Pex5p tetramer. In this Pex5p–Pex20p complex, the conformation of tetrameric Pex5p had changed from a closed conformation with a diameter of 115 Å into an open conformation of 134 Å. EM also indicated that the Pex5p–Pex20p complex was capable to bind native, folded catalase, a peroxisomal PTS1 protein. This suggests that the Pex5p–Pex20p complex may be functional as receptor complex.