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. © 2010 European Molecular Biology Organization | All Rights Reserved.
CITATION STYLE
Schueller, N., Holton, S. J., Fodor, K., Milewski, M., Konarev, P., Stanley, W. A., … Wilmanns, M. (2010). The peroxisomal receptor Pex19p forms a helical mPTS recognition domain. EMBO Journal, 29(15), 2491–2500. https://doi.org/10.1038/emboj.2010.115
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