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Submitted on October 25, 2001
Revised on January 21, 2002
Accepted on February 20, 2002

Analysis of mammalian peroxin interactions using a non-transcription-based bacterial two-hybrid assay

Marc Fransen, Chantal Brees, Karen Ghys, Leen Amery, Guy P. Mannaerts, Daniel Ladant, and Paul P. Van Veldhoven

Farmacologie, Katholieke Universiteit Leuven, Leuven, Vlaams-Brabant 3000

Corresponding Author: marc.fransen{at}med.kuleuven.ac.be

In recent years, substantial progress has been made in the identification of proteins involved in peroxisome biogenesis. However, with the exception of the peroxisome-targeting signal (PTS) receptors and the receptor docking proteins, the function of most of these proteins, called peroxins, remains largely unknown. One step toward elucidating a protein’s function is to identify its interacting partners. We have used a non-transcription-based bacterial two-hybrid system (b-2HS) to analyze the interactions between a set of 12 mammalian peroxins, and a yeast protein three-hybrid system (y-3HS) to investigate whether or not proteins that interact with the same peroxin and have overlapping binding sites cooperate or compete for this site. Here we report a detailed interaction map of these peroxins and demonstrate that (i) farnesylation, and not the CaaX motif, of Pex19p strongly enhances its affinity for Pex13p, (ii) the CaaX motif, and not farnesylation, of Pex19p strongly enhances its affinity for Pex11pb, and (iii) the C3HC4 RING finger domain of Pex12p does not alter the binding properties of Pex5p for the C-terminal peroxisome-targeting signal PTS1. Finally, we show that the Pex5p-Pex13p interaction is bridged by Pex14p, and that the latter molecule exists predominantly as a dimer in vivo. Collectively, as demonstrated in this work with peroxins, these results indicate that the b-2HS is an attractive complementary approach to the conventional transcription-based yeast two-hybrid system (y-2HS) for studying protein-protein interactions.


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