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Updated: Jul 10, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
A conserved alpha helical domain at the N-terminus of Pex14p is required for PTS1 and PTS2 protein import in
Bart de Vries1, Jan A K W Kiel, Ruud Scheek
1Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, 9750 AA, Haren, The Netherlands.
Abstract:
We have analyzed the highly conserved N-terminus of Hansenula polymorpha Pex14p for its function in peroxisomal matrix protein import. The region comprising aa 10-54 of HpPex14p is predicted to contain three alpha-helices. Its alpha-helical structure was confirmed by CD analysis of a synthetic peptide, corresponding to residues 8-58. Deletion of aa 1-21 of HpPex14p, but not of aa 1-9, completely abolished PTS1 and PTS2 matrix protein import. An extensive mutational analysis of the first alpha-helix (aa 10-21) demonstrated that its secondary structure, as well as residues Phe20 and Leu21, are essential for PTS1 and PTS2 matrix protein import.
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