The peroxisomal receptor Pex19p forms a helical mPTS recognition domain

Nicole Schueller, Simon J. Holton, Krisztian Fodor, Morlin Milewski, Petr Konarev, Will A. Stanley, Janina Wolf, Ralf Erdmann, Wolfgang Schliebs, Young Hwa Song, Matthias Wilmanns*

*Corresponding author for this work
45 Citations (Scopus)


The protein Pex19p functions as a receptor and chaperone of peroxisomal membrane proteins (PMPs). The crystal structure of the folded C-terminal part of the receptor reveals a globular domain that displays a bundle of three long helices in an antiparallel arrangement. Complementary functional experiments, using a range of truncated Pex19p constructs, show that the structured α-helical domain binds PMP-targeting signal (mPTS) sequences with about 10 μM affinity. Removal of a conserved N-terminal helical segment from the mPTS recognition domain impairs the ability for mPTS binding, indicating that it forms part of the mPTS-binding site. Pex19p variants with mutations in the same sequence segment abolish correct cargo import. Our data indicate a divided N-terminal and C-terminal structural arrangement in Pex19p, which is reminiscent of a similar division in the Pex5p receptor, to allow separation of cargo-targeting signal recognition and additional functions.

Original languageEnglish
JournalEMBO Journal
Issue number15
Pages (from-to)2491-2500
Number of pages10
Publication statusPublished - 04.08.2010


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