Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5pSchäfer, A., Kerssen, D., Veenhuis, M., Kunau, W-H. & Schliebs, W., 2004, In : Molecular and Cellular Biology. 24, 20, p. 8895 - 8906 12 p.
Research output: Contribution to journal › Article › Academic › peer-review
Within the extended receptor cycle of peroxisomal matrix import, the function of the import receptor Pex5p comprises cargo recognition and transport. While the C-terminal half (Pex5p-C) is responsible for PTS1 binding, the contribution of the N-terminal half of Pex5p (Pex5p-N) to the receptor cycle has been less clear. Here we demonstrate, using different techniques, that in Saccharomyces cerevisiae Pex5p-N alone facilitates the import of the major matrix protein Fox1p. This finding suggests that Pex5p-N is sufficient for receptor docking and cargo transport into peroxisomes. Moreover, we found that Pex5p-N can be functionally replaced by Pex18p, one of two auxiliary proteins of the PTS2 import pathway. A chimeric protein consisting of Pex18p (without its Pex7p binding site) fused to Pex5p-C is able to partially restore PTS1 protein import in a PEX5 deletion strain. On the basis of these results, we propose that the auxiliary proteins of the PTS2 import pathway fulfill roles similar to those of the N-terminal half of Pex5p in the PTS1 import pathway.
|Pages (from-to)||8895 - 8906|
|Number of pages||12|
|Journal||Molecular and Cellular Biology|
|Publication status||Published - 2004|
- TARGETING SIGNAL RECEPTOR, TETRATRICOPEPTIDE REPEAT-DOMAIN, YEAST YARROWIA-LIPOLYTICA, SACCHAROMYCES-CEREVISIAE, PICHIA-PASTORIS, MATRIX PROTEIN, SH3 DOMAIN, 3-OXOACYL-COA THIOLASE, MEMBRANE-PROTEINS, IMPORT MACHINERY