The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain

• Type: Article in International Scientific Journal
• Date: 2006

Authors

carvalho, af (Author) Other; costa-rodrigues, j (Author) FMDUP; correia, i (Author) Other; pessoa, jc (Author) Other; faria, tq (Author) Other; martins, cl (Author) Other; fransen, m (Author) Other; sa-miranda, c (Author) Other; azevedo, je (Author) ICBAS

Journal

Title: Journal of Molecular Biology

Vol. 356 No. 4

Pages: 864-875

ISSN: 0022-2836

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 48 Citations

Scopus - 40 Citations

Other information

Authenticus ID: P-004-MT0

DOI: 10.1016/j.jmb.2005.12.002

Abstract (EN): Targeting of most newly synthesised peroxisomal matrix proteins to the organelle requires Pex5p, the so-called PTS1 receptor. According to current models of peroxisomal biogenesis, Pex5p interacts with these proteins in the cytosol, transports them to the peroxisomal membrane and catalyses their translocation across the membrane. Presently, our knowledge on the structural details behind the interaction of Pex5p with the cargo proteins is reasonably complete. In contrast, information regarding the structure of the Pex5p N-terminal half (a region containing its peroxisomal targeting domain) is still limited. We have recently observed that the Stokes radius of this Pex5p domain is anomalously large, suggesting that this portion of the protein is either a structured elongated domain or that it adopts a low compactness conformation. Here, we address this issue using a combination of biophysical and biochemical approaches. Our results indicate that the N-terminal half of Pex5p is best described as a natively unfolded premolten globule-like domain. The implications of these findings on the mechanism of protein import into the peroxisome are discussed.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12