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By genome analysis, we previously identified Pex14⁄17p as a putative novel peroxin ofPenicillium chrysogenum. Here, we show that Pex14⁄17p is a component of the peroxisomal membrane that is essential for efficient per-oxisomal targeting signal 1 and peroxisomal targeting signal 2 matrix pro-tein import, implying that the protein is indeed a genuine peroxin. Additionally, aPEX14⁄17deletion strain is affected in conidiospore forma-tion. | Penicillium chrysogenum Pex14 17p - a novel component of the peroxisomal membrane that is important for penicillin production Lukasz Opalinski1 2 Jan A. K. W. Kiel1 2 Tim G. Homan1 2 Marten Veenhuis1 2 and Ida J. van der Klei1 2 1 Molecular CellBiology Groningen Biomolecular Sciences and Biotechnology Institute GBB University of Groningen Haren The Netherlands 2 Kluyver Centre for Genomics of IndustrialFermentation Delft The Netherlands Keywords antibiotic production fungi peroxisome protein sorting sporulation Correspondence I. J. van der Klei Molecular CellBiology Groningen Biomolecular Sciences and Biotechnology Institute GBB PO Box 14 NL-9750 AA Haren The Netherlands Fax 31 50 363 8280 Tel 31 50 363 2179 E-mail I.J.van.der.klei@rug.nl These authors contributed equally to this work Received 25 September 2009 revised 13 April 2010 accepted 1 June 2010 doi 10.1111 j.1742-4658.2010.07726.x By genome analysis we previously identified Pex14 17p as a putative novel peroxin of Penicillium chrysogenum. Here we show that Pex14 17p is a component of the peroxisomal membrane that is essential for efficient peroxisomal targeting signal 1 and peroxisomal targeting signal 2 matrix protein import implying that the protein is indeed a genuine peroxin. Additionally a PEX14 17 deletion strain is affected in conidiospore formation. Pex14 17p has properties of both Pex14p and Pex17p in that the N-terminus of this protein is similar to the highly conserved Pex5p-binding region present in the N-termini of Pex14p proteins whereas its C-terminus shows weak similarity to yeast Pex17p proteins. We have identified a novel motif in both Pex17p and Pex14 17p that is absent in Pex14p. We show that an N-terminally truncated but not a C-terminally truncated Pex14 17p is able to complement both the matrix protein import and sporulation defects of a Dpex14 17 strain implying that it is the Pex17p-related portion of the protein that is crucial for its function as a peroxin. Possibly this .
